Roche

2.7.7.7 ( BRENDA | IUBMB )

The enzyme was cloned in E.coli and is isolated to be free of unspecific endo- or exonucleases according to the current quality control procedurese. Taq DNA Polymerase is a highly processive 5–3 DNA polymerase that lacks 3–5 exonuclease activity. It consists of a single polypeptide chain with a molecular weight of approximately 95 kDa. The enzyme exhibits highest activity at a pH of around 9 (adjusted at 20 °C) and temperatures around +75 °C. Taq DNA Polymerase also accepts modified deoxyribonucleosidetriphosphates as substrates, and can be used to label DNA-fragments either with radionucleotides, digoxigenin, fluorescein or biotin.
The high processivity, absence of exonuclease activity and temperature optima of Taq DNA Polymerase enable the use of this enzyme in DNA sequencing, especially where the resolution of secondary structures plays a major role.

This lower concentration of our recombinant Taq DNA Polymerase allows small amounts of the polymerase to be pipetted more accurately and conveniently. In all other respects, this preparation is identical to our higher concentration (5 U/µl) preparation and can be used for:

PCR
RT-PCR
Other primer-extension reactions, such as sequencing and labeling

Packaging
1 kit containing 4 components
Unit Definition
One unit Taq DNA Polymerase is defined as the amount of enzyme that incorporates 10 nmol of total deoxyribonucleoside triphosphates into acid precipitable DNA within 60 min at +65 °C under the assay conditions stated above.
Unit Assay: Incubation buffer:
67 mM Tris/HCl; pH 8.3/25 °C, 5 mM MgCl2, 10 mM Mercaptoethanol, 0.2% Polydocanol, 0.2 mg/ml Gelatine, 0.2 mM each dATP, dGTP, dTTP and 0.1 mM dCTP.
Incubation procedure:
M13mp9ss, M13 primer (17mer) and 1 µCi (-32P) dCTP are incubated with suitable dilutions of Taq DNA Polymerase in 50 µl incubation buffer at +65 °C for 60 minutes. The amount of incorporated dNTPs is determined by trichloroacetic acid precipitation.
Volume Activity: 1 U/µl

For life science research only. Not for use in diagnostic procedures.

Use of this product is covered by US patent claims and corresponding patent claims outside the US. The purchase of this product includes a limited, non-transferable immunity from suit under the foregoing patent claims for using only this amount of product for the purchaser′s own internal research. No right under any other patent claim, no right to perform any patented method, and no right to perform commercial services of any kind, including without limitation reporting the results of purchaser′s activities for a fee or other commercial consideration, is conveyed expressly, by implication, or by estoppel. This product is for research use only. Diagnostic uses under Roche patent claims require a separate license from Roche. Further information on purchasing licenses may be obtained by contacting the Director of Licensing, Applied Biosystems, 850 Lincoln Centre Drive, Foster City, California 94404, USA.

usage	sufficient for ≤2,000 reactions (11647687001), sufficient for ≤500 reactions (11647679001)
Quality Level	100,
feature	dNTPs included: no, hotstart: no
packaging	pkg of 1,000 U (11647687001 [4 x 250 U]), pkg of 250 U (11647679001)
Торговая марка	Roche
parameter	72 °C optimum reaction temp.
application(s)	PCR: suitable
optimum pH	~9.0 (20 °C)
shipped in	dry ice
storage temp.	−20°C

Узнать цену

Подробнее

Taq DNA Polymerase, 5 U/l

2.7.7.7 ( BRENDA | IUBMB )

Taq DNA Polymerase is a highly processive 53 DNA polymerase that lacks 35 exonuclease activity. It is a single polypeptide chain with a molecular weight of approximately 95 kDa.
Taq DNA Polymerase was originally isolated from the thermophilic eubacterium Thermus aquaticus BM, a strain lacking Taq I restriction endonuclease. The enzyme was cloned in E.coli.

Taq DNA Polymerase can be used in simple, routine PCR. Roche Applied Science Taq DNA polymerase is held to rigorous purity and quality standards. This preparation of recombinant Taq DNA Polymerase can be applied for:

PCR
RT-PCR
qPCR
Other primer-extension reactions, such as sequencing and labeling

Features and Benefits
Reliable reproducible results:
High lot-to-lot consistency.
No need to test each lot:
Taq DNA Polymerase is rigorously tested.
Prevent PCR carryover:
dUTP incorporation combination with Uracil-DNA Glycosylase prevents PCR cross-contamination.
Packaging
1 kit containing 2 components
Quality
Routine assays have medium size amplicons and 50% GC content. Taq DNA Polymerase has no proofreading or hot start features. It is optimally active at +75°C and pH 9.
Lack of restriction endonuclease:
The enzyme originally isolated from T. aquaticus BM lacks Taq I restriction endonuclease activity.Each lot is PCR tested using DNA. Each lot is also tested for the absence of exo- and endonucleases, and nicking activities according to the current Quality Control procedures.
Unit Definition
One unit Taq DNA Polymerase is defined as the amount of enzyme that incorporates 10 nmol of total deoxyribonucleosidetriphosphates into acid precipitable DNA within 60 min at +65 °C under the assay conditions given above.
Unit Assay: Incubation buffer:
67 mM Tris/HCl; pH 8.3/25 °C, 5 mM MgCl2, 10 mM Mercaptoethanol, 0.2% Polydocanol, 0.2 mg/ml Gelatine, 0.2 mM each dATP, dGTP, dTTP and 0.1 mM dCTP.
Incubation procedure:
M13mp9ss, M13 primer (17mer) and 1 µCi (-32P) dCTP are incubated with suitable dilutions of Taq DNA Polymerase in 50 µl incubation buffer at +65 °C for 60 minutes. The amount of incorporated dNTPs is determined by trichloroacetic acid precipitation.
Volume Activity: 5 U/µl

For life science research only. Not for use in diagnostic procedures.

usage	sufficient for ≤1,000 reactions (11146173001), sufficient for ≤10,000 reactions (11435094001), sufficient for ≤2,000 reactions (11418432001), sufficient for ≤5,000 reactions (11596594001), sufficient for ≤200 reactions (11146165001)
Quality Level	100,
packaging	pkg of 1,000 U (11418432001 [4 x 250 U]), pkg of 2,500 U (11596594001 [10 x 250 U]), pkg of 5,000 U (11435094001 [20 x 250 U]), pkg of 100 U (11146165001), pkg of 500 U (11146173001 [1 x 500 U])
Торговая марка	Roche
parameter	72 °C optimum reaction temp.
optimum pH	~9.0 (20 °C)
shipped in	dry ice
storage temp.	−20°C

Узнать цену

Подробнее

Taq DNA Polymerase, GMP Grade 3734927001

2.7.7.7 ( BRENDA | IUBMB )

Taq DNA Polymerase, GMP Grade, is manufactured under GMP conditions. It also fulfills the high quality and documentation requirements of research and development laboratories in the pharmaceutical and biotechnology industries. Taq DNA Polymerase, GMP Grade, gives high lot-to-lot consistency. Recombinant Taq DNA Polymerase (from Thermus aquaticus, recombinant E. coli), GMP Grade, is a highly processive 5–3 DNA polymerase that lacks 3–5 exonuclease activity. The thermostable enzyme is a single polypeptide chain with a molecular weight of approximately 95 kD. Taq DNA Polymerase also accepts modified deoxyribonucleoside triphosphates as substrates for highly efficient DNA labeling with radionucleotides, digoxigenin, fluorescein, or biotin.

Packaging
1 kit containing 2 components
Unit Definition
One unit Taq DNA Polymerase, GMP Grade is defined as the amount of enzyme that incorporates 20 nmol of total deoxyribonucleoside-triphosphates into acid precipitable DNA within 60 minutes at +65 °C under the assay conditions stated in the package insert.
Unit Assay: Incubation buffer for assay on activated DNA:
67 mM Tris/HCl; pH 8.3/25 °C, 5 mM MgCl2, 10 mM mercaptoethanol, 0.2% polydocanol, 0.2 mg/ml gelatine, 0.2 mM each dATP, dGTP, dTTP and 0.1 mM dCTP, pH 8.3 (25 °C).
Incubation procedure:
M13mp9ss, M13 primer (17mer) and 1 µCi [-32P]-dCTP are incubated with suitable dilutions of Taq DNA Polymerase in 50 µl incubation buffer at 65 °C for 60 min. The amount of incorporated dNTPs is determined by trichloroacetic acid precipitation.
Volume Activity: 5 U/µl

Taq DNA Polymerase, GMP Grade, can be applied for:
PCR
RT- PCR
Other primer-extension reactions, such as sequencing and labeling

For life science research only. Not for use in diagnostic procedures.

Quality Level	100,
assay	>98% (SDS-PAGE)
usage	sufficient for 2,000 reactions
specific activity	13000 units/mg protein
feature	Difficult Templates/Specialty Enzymes PCR, dNTPs included: no, hotstart: no
packaging	pkg of 1,000 U
Торговая марка	Roche
parameter	72 °C optimum reaction temp.
application(s)	PCR: suitable
input	purified DNA
optimum pH	~9 (20 °C)
shipped in	dry ice
storage temp.	20°C (15°C to 25°C)

hcodes	H412
pcodes	P273 - P501
RIDADR	NONH for all modes of transport
WGK Germany	WGK 2
Flash Point F	does not flash
Flash Point C	does not flash

Узнать цену

Подробнее

TeloTAGGG™ Telomerase PCR ELISA 11854666910

Photometric enzyme immunoassay for the detection of telomerase activity, utilizing the Telomeric Repeat Amplification Protocol (TRAP).
Telomeres are specialized DNA protein structures found at the end of eukaryotic chromosomes. Telomeric DNA is characterized by an array of tandemly repeated, G-rich DNA sequences (six nucleotides in length) that are highly conserved during evolution (human repeat sequence: TTAGGG). As DNA polymerase a is unable to replicate the very ends of linear DNA, every replication cycle leads to a progressive shortening of the telomeric ends in normal somatic cells. This phenomenon appears to be linked to the limited proliferative capacity of normal somatic cells of higher eukaryotes. Telomerase, a ribonucleoprotein, catalyzes the addition of TTAGGG repeats to the ends of vertebrate chromosomes, using a complementary sequence of its intrinsic RNA component as a template. Telomerase activity has been shown to be expressed in germ cells, as well as most cell lines and tumors. Escaping from the proliferative limitations of cellular senescence, telomerase reactivation may be a prerequisite of the development of malignant tumor cells from somatic cells.

The TeloTAGGG™ Telomerase PCR ELISA is designed for use in life science research studies for the highly sensitive qualitative detection of telomerase activity in cell extracts from cell cultures and other biological samples. The TeloTAGGG Telomerase PCR ELISA utilizes a single-tube reaction mixture that simplifies the amplification reaction. The ELISA technique uses a biotinylated primer to immobilize the TRAP reaction products within a streptavidin-coated microplate, and a specific DIG-labeled probe for detection.
Features and Benefits

Easy: One-step/one-tube ready-to-use reaction mix for elongation and amplification. Detection of up to 96 samples in an ELISA format without laborious gel separation.
Reliable: Shows high correlation with standard TRAP assay
Safe: Nonradioactive method that can be performed in any laboratory
Complete: All components necessary for elongation, amplification, and detection are provided in the kit

Assay time: Approximately 5 - 8 hours
Sample material: Cell or tissue extracts
Sensitivity: As sensitive as the radioactive (or isotopic) TRAP assay
Packaging
1 kit containing 15 components.
Principle
In detecting telomeric activity, a sample that contains telomerase will add these repetitive sequences to the 3′-end of the biotinylated synthetic P1-TS-primer (primer and nucleotides in Reaction mixture, bottle 2). In a second step, these elongated products are amplified by PCR using the primers P1-TS and P2, generating PCR amplicons. The Telomerase PCR ELISA combines both reactions in a one-step/ one-tube reaction. Optimized primer sequences eliminate the need for hot start PCR or the use of a wax barrier, and avoids amplification artifacts, such as primer dimers. An aliquot of the PCR is denatured and hybridized to a digoxigenin (DIG)-labeled, telomeric repeat-specific detection probe (contained in the Hybridization buffer, bottle 4). The hybridization products are immobilized via the biotin-labeled primer to a streptavidin-coated microplate. The immobilized PCR product is detected with an anti-digoxigenin antibody conjugated to peroxidase. The probe is finally visualized by peroxidase, which metabolizes TMB to form a colored reaction product. As an alternative to the ELISA protocol, the biotinylated primer may also be used for detection. If the telomerase-mediated six nucleotide incremental ladder is desired, fragments may be separated by PAGE, blotted onto a positively charged membrane, then detected appropriately (Biotin Luminescent Detection Kit).
Preparation Note
Working solution: Solution 5: Washing buffer, 1x
Dilute an appropriate volume of Washing buffer, 10x conc. with autoclaved double-dist. water (1:10) and mix thoroughly. Approx. 2.5 ml of the diluted Washing buffer are needed for one reaction.
Solution 6: Anti-DIG peroxidase, stock solution
Reconstitute the lyophilizate in 240 µl autoclaved double-dist. water. This results in an antibody conjugate concentration of 0.5 U/ml.
Solution 10: Positive control, cell extract
Reconstitute lyophilized cell extract on ice with 20 µl autoclaved double-dist. water (optionally treated with DEPC- or Velcorin) and mix thoroughly. The reconstituted solution has a concentration of about 1 x 103 cell equivalents per microliter.
Dispense solution into suitable aliquots (1 to 3 µl will be needed for 1 reaction).
Keep the extract on ice during pipetting.
Storage conditions (working solution): Washing buffer,1x:
Stable at 2 to 8 °C for 1month.
Anti-DIG peroxidase, stock solution:
Stable at 2 to 8 °C for 6 months.Do not freeze. Do not add sodium azid.
Anti-DIG peroxidase, working solution:
Prepare immediately before use. Do not store.
Positive control,cell extract:
The aliquoted cell extract is stable at -80 °C until the expiration date printed on the label. Avoid repeated freezing and thawing.

For life science research only. Not for use in diagnostic procedures.

Manufactured under license from Geron Corporation.
TeloTAGGG is a trademark of Roche

Quality Level	100,
usage	sufficient for 96 reactions
Торговая марка	Roche
shipped in	dry ice
storage temp.	20°C

pictograms	GHS05,GHS07
signalword	Warning
hcodes	H290 - H317
pcodes	P261 - P280 - P333 + P313 - P362 + P364 - P390 - P501
RIDADR	UN 3316 9
WGK Germany	WGK 2
Flash Point F	does not flash
Flash Point C	does not flash

Узнать цену

Подробнее

TeloTAGGG™ Telomerase PCR ELISAPLUS 12013789001

The TeloTAGGG Telomerase PCR ELISAPLUS kit provides a way to perform a highly sensitive photometric enzyme immunoassay to detect telomerase activity, using nonradioactive techniques. The TeloTAGGG Telomerase PCR ELISAPLUS is designed for use in life science research studies in cell extracts from cell cultures and other biological research samples. The TeloTAGGG Telomerase PCR ELISAPLUS utilizes single-tube reaction mixtures, similar to the TeloTAGGG Telomerase PCR ELISA, but also contains an optimized internal standard and control template, which allows the TeloTAGGG Telomerase PCR ELISAPLUS to quantitatively measure the amount of telomerase reaction product. It uses the Telomeric Repeat Amplification Protocol (TRAP).

The TeloTAGGG Telomerase PCR ELISAPLUS has been used to detect telomerase activity in urine, frozen sections of head and neck squamous cell carcinomas and tumor margin tissues.
Features and Benefits

Ready-to-use master mixes: the kit contains all of the essential compounds as master mixes
Reliability: Positive control contained in the kit
Specificity: The use of hybridization probes ensures specific detection of the applied telomerase reaction product
Quantitative results: The assay concept allows semi-quantitative determination of telomerase levels

Packaging
1 kit containing 16 components.
Specifications
Assay time: Approximately 7 hours
Measuring range: The linear measuring range of the kit is from 10 - 2,000 cells (in a model system using 293 cells)
Sample material: Cell cultures and biological research samples
Sensitivity: Detects <10 cell equivalents (in a model system, using 293 cells)
Principle
The test principle can be divided into the following steps:
Step 1: Elongation/amplification
In the first step, telomerase adds telomeric repeats (TTAGGG) to the 3-end of the biotin-labeled synthetic P1-TS primer. These elongation products, as well as the Internal standard (IS) included in the same reaction vessel, are amplified by PCR using the primers P1-TS and the anchor-primer P2. PCR products derived from telomerase-mediated elongation products in the first step contain the telomerase-specific six nucleotide increments, while the Internal standard (IS) generates a 216-bp PCR product.
Step 2: Detection by ELISA
The PCR products are split into two aliquots, denatured, and hybridized separately to digoxigenin-(DIG)-labeled detection probes that are specific for the telomeric repeats (P3-T) and for the Internal standard (IS) (P3-Std), respectively. The resulting products are immobilized via the biotin label to a streptavidin-coated microplate. Immobilized amplicons are then detected with an antibody against digoxigenin, which is conjugated to horseradish peroxidase (Anti-DIG-HRP) and the sensitive peroxidase substrate TMB.
Preparation Note
Working solution: Solution 10: Washing Buffer, 1x
Dilute an appropriate volume of Washing buffer, 10x concentrated (bottle 10) with autoclaved double-distilled water (1:10) and mix thoroughly. Approximately 5 ml of the diluted Washing buffer are needed for one reaction.
Stable at 2 to 8 °C for 1 month.
Solution 11: Anti-DIG HRP, bottle 11 stock solution
Reconstitute the lyophilizate in 240 µl autoclaved double-distilled water. This results in an antibody conjugate concentration of 0.5 U/ml.
Stable at 2 to 8 °C for 6 months. Do not freeze! Do not add sodium azide!
Solution 11: Anti-DIG HRP, working solution
To prepare the working solution, dilute an appropriate amount of the reconstituted anti-DIG-HRP (solution 11) with Conjugate dilution buffer (solution 12) to a final concentration of 10 mU/ml (e.g., 200 µl antibody solution and 9.8 ml of Conjugate dilution buffer).
Prepare immediately before use. Do not store.
Storage conditions (working solution): Washing buffer, 1x:
Stable at 2 to 8 °C for 1 month.
Anti-DIG HRP, stock solution:
Stable at 2 to 8 °C for 6 months. Do not freeze. Do not add sodium azide.
Anti-DIG HRP, working solution:
Prepare immediately before use. Do not store.

For life science research only. Not for use in diagnostic procedures.

Manufactured under license from Geron Corporation.
TeloTAGGG is a trademark of Roche

Quality Level	100,
usage	sufficient for 96 reactions
Торговая марка	Roche
shipped in	dry ice
storage temp.	20°C

pictograms	GHS05,GHS07
signalword	Warning
hcodes	H290 - H317
pcodes	P261 - P280 - P333 + P313 - P362 + P364 - P390 - P501
RIDADR	UN 3316 9
WGK Germany	WGK 2
Flash Point F	does not flash
Flash Point C	does not flash

Узнать цену

Подробнее

TeloTAGGG™ Telomere Length Assay 12209136001

Telomeres, the specialized DNA protein structures located at the end of eukaryotic chromosomes, consist of small, tandemly repeated DNA sequences. Numerous telomere sequences have been identified that display very few sequence variations, even between phylogenetically divergent organisms such as Tetrahymena (sequence: TTGGGG) and humans (sequence: TTAGGG).
Because DNA polymerase is unable to replicate the very ends of linear DNA, it was suggested that chromosomal ends progressively shorten with each replication cycle (called the “end-replication problem”). This phenomenon, which has been demonstrated in vitro and in vivo, seems to be linked to the limited proliferative capacity of normal somatic cells (“mitotic clock”). Since germ-line cells, stem cells, and tumor cells all exhibit a prolonged or even infinite life span, it was suggested that these cells must possess a particular mechanism for maintaining telomere length.
Maintaining stable telomere length is associated with the activation of telomerase. This enzyme is a ribonucleoprotein that compensates for the loss of telomeric DNA by adding repeat sequences to the chromosome ends, using its intrinsic RNA component as a template for DNA synthesis.
Telomeres play an essential role in the stable maintenance of eukaryotic chromosomes within a cell by specifically binding to structural proteins. These proteins cap the ends of linear chromosomes, preventing nucleolytic degradation, end-to-end fusion, irregular recombination, and other events that are normally lethal to a cell.
Analysis of telomere length in research samples of human peripheral blood mononuclear cells reveals that telomere length decreases with increased age in the donor, reflecting the replicative history of those cells. In several disorders (e.g., Downs syndrome, ataxia telangiectasia, and HIV infection), accelerated telomere loss has been described, suggesting the reduction in telomere length may be related to the immune dysfunction associated with these disorders. This kit is intended to increase scientific knowledge about these relationships.
Assay time: Approximately 18 hours
Sample material: Cell cultures and other biological samples
Nonradioactive chemiluminescent assay to determine telomere length.
The kit utilizes Southern analysis of terminal restriction fragments (TRF) that are obtained by the digestion of genomic DNA using frequently cutting restriction enzymes.
Step 1: Digestion of genomic DNA
Purified genomic DNA is digested by an optimized mixture of frequently cutting restriction enzymes. The enzymes have been selected in such a way that telomeric DNA and sub-telomeric DNA is not cut. This is due to the special sequence characteristics of the repeats. Non-telomeric DNA is digested to low molecular-weight fragments.
Step 2: Gel electrophoresis and Southern blotting
Following DNA digestion, the DNA fragments are separated by gel electrophoresis, then transferred to a nylon membrane by Southern blotting.
Step 3: Hybridization and chemiluminescence detection
The blotted DNA fragments are hybridized to a digoxigenin (DIG)-labeled probe that is specific for telomeric repeats, then incubated with a DIG-specific antibody covalently coupled to alkaline phosphatase. Finally, the immobilized telomere probe is visualized by a highly sensitive chemiluminescent substrate for alkaline phosphatase, CDP-Star. The average TRF length can be determined by comparing the signals to a molecular-weight standard.

The TeloTAGGG™ Telomere Length Assay is designed for use in the following life science research applications:

Sensitive detection of telomeric DNA (telomeric sequence: TTAGGG) in cell cultures and other biological research samples
Determination of the telomere length of DNA in cell cultures and other biological research samples

Packaging
1 kit containing 15 components.
Sequence
Sequence and length of the probe are confidential. The DIG labeled MW in the Kit is a mixture of DIG MW III and VII
Preparation Note
Working concentration: Working concentration of conjugate depends on application and substrate
The following concentrations should be taken as a guideline:

Safe: Nonradioactive
Flexible: Detects telomeres from a variety of organisms, including humans and mice

Dot blot: 100 ng/ml
ELISA: 100 ng/ml
Western blot: 100 ng/ml

For life science research only. Not for use in diagnostic procedures.

Manufactured under license from Geron Corporation.
TeloTAGGG is a trademark of Roche

Quality Level	100
usage	sufficient for 50 reactions
mfr. no.	Roche
shipped in	dry ice
storage temp.	20°C

Thrombin 10602400001

3.4.21.5 ( BRENDA | IUBMB )

Thrombin is a Na+ activated allosteric serine protease. It belongs to chymotrypsin family. Thrombin is made of two polypeptide chains of 36 (A chain) and 259 (B chain) residues that are covalently attached with a disulfide bond.
Thrombin is a coagulation factor IIa. It is a serine endopeptidase that hydrolyzes peptide and ester bonds specifically at the carboxylic side of Arg. The enzyme converts fibrinogen to fibrin. The product contains EDTA and additional stabilizing agents.

Thrombin is used in coagulation research, medical research, protein-structure analysis, and biochemical research. It has been used for the stimulation of the platelets.
Thrombin has been used in the expression and purification of recombinant RELM (resistin-like moleculefamily members. It has also been used in platelet spreading on fibrinogen and immunostaining.
Biochem/physiol Actions
Thrombin plays an important role in blood coagulation. It serve as a procoagulant factor while transforming fibrinogen into an insoluble fibrin clot. Thrombin can act as anticoagulant by the activation of protein C.
Physical form
Lyophilizate
Preparation Note
Storage conditions (working solution): -15 to -25°C
Inhibitors: DFP, TLCK, PMSF, benzamidine, 1-antitrypsin, 2-macroglobulin, antithrombin III heparin, hirudin, and APMSF
Reconstitution
The reconstituted solution contains 20 mM EDTA.
Important note:
Use plastic vials and pipettes because thrombin will be adsorbed to glass surfaces!
Storage and Stability
Store at 2 to 8 °C. (Store dry!)

For life science research only. Not for use in diagnostic procedures.

Quality Level	100,
form	lyophilized
specific activity	~120 units/mg protein (At 25 °C with Chromozym TH as the substrate.)
mol wt	M_r ~33.6 kDa
packaging	pkg of 20 U
Торговая марка	Roche
optimum pH	8.2-9.0
shipped in	wet ice

pictograms	GHS07
signalword	Warning
hcodes	H332
pcodes	P261 - P271 - P304 + P340 + P312
RIDADR	NONH for all modes of transport
WGK Germany	WGK 2
Flash Point F	does not flash
Flash Point C	does not flash

Transcriptor Universal cDNA Master 5893151001

Ready-to-use reaction mix for two-step RT-qPCR on all real-time PCR systems.
The Transcriptor Universal cDNA Master is the convenient solution for time-saving cDNA synthesis for two-step real-time RT-PCR. All reagents required, including random hexamer primer, nucleotides, buffers and enzymes are supplied in just two vials minimizing pipetting. Maximum convenience is achieved by combining the Transcriptor Universal cDNA Master mix with the RealTime ready Cell Lysis Kit, further accelerating real-time PCR by directly using cell lysates. The unique enzyme included in this kit has a broad temperature range and is suitable for high temperature reverse transcription. The Transcriptor Universal cDNA Master produces very high specificity and sensitivity, even with difficult complex RNA templates. Excellent performance and linear response in real-time RT-PCR is obtained for both low and high copy genes. The Transcriptor Universal cDNA Master is compatible with LightCycler® instruments and all other real-time PCR instruments requiring normalization with a reference dye.
Sensitive and accurate RT-PCR assay is a prerequisite for meaningful molecular genetic analyses. Choosing the correct enzyme for reverse transcription and cDNA synthesis is critical for obtaining high yields of high quality full-length cDNA, that is faithful to the original cellular RNA.
We offer a comprehensive selection of Transcriptor reverse transcription products, including:

Enzymes with exquisite performance and broad dynamic range in real-time PCR.
Enzymes for high temperature reverse transcription to synthesize cDNA from RNA with secondary structures.
High Fidelity Transcriptor products, with proofreading activity, for applications requiring the highest sequence accuracy.

Reverse transcription is a hallmark of molecular biology. The ability to convert RNA into DNA for qualitative and quantitative RNA analysis using PCR or real-time PCR has revolutionized gene expression analysis. Quantitative reverse transcription polymerase chain reaction (RT-PCR or qRT-PCR) is now the standard for mRNA detection and quantification, sensitive enough to quantify RNA from a single cell.
RT-PCR is also used for the creation of cDNA libraries, molecular cloning by PCR, and sequencing. The Transcriptor Universal cDNA Master is a convenient fast solution for cDNA synthesis and real-time PCR analysis. No matter which PCR instrument you are using, this master mix, supplied in just two vials, brings out the full potential of your qRT-PCR assays.
Features and Benefits

Conserve valuable resources with effortless setup.

Just add your RNA. The two vials included in this kit contain all reagents required for reverse transcription, including random hexamer primer, nucleotides, buffers and enzymes

Save time with a fast protocol.

The optimized master mix significantly reduces reverse transcription times (10 minutes) and setup times.

Maximize convenience by combining this master mix with the Roche RealTime ready Cell Lysis Kit for cell lysates without RNA purification.
Power through the most difficult templates.

Transcriptor Reverse Transcriptases high thermostability and specially optimized buffer system permit incubation temperatures up to +60°C, accurately transcribing even the most challenging secondary structures.

Reliably standardize and quantify your qRT-PCR experiments.

Obtain sensitive reproducible results over a linear dynamic range of at least six orders of magnitude.

Increase the sensitivity and specificity of your two-step qRT-PCR.

Produce lower cycle threshold (Ct) values, starting with target amounts as low as 0.1 pg total RNA.
Components

Transcriptor Universal Reverse Transcriptase, 20x concentrated
Transcriptor Universal Reaction Buffer, 5x concentrated

For life science research only. Not for use in diagnostic procedures.
Reverse Transcriptases Overview,

Quality Level	100,
usage	sufficient for 100 reactions
feature	dNTPs included: no
Торговая марка	Roche
packaging	kit of for 100 reactions
application(s)	RT-qPCR: suitable
input	purified RNA
detection method	probe-based

RIDADR	NONH for all modes of transport
WGK Germany	WGK 1
Flash Point F	does not flash
Flash Point C	does not flash

Transferrin 10652202001

Transferrin is a serum glycoprotein that participates in the transport of iron from absorption and storage sites to tissue cells. The iron-bound transferrin, also referred to as ferrotransferrin, binds to specific cell surface receptors on growing cells and are internalized by endocytosis. Once inside, the iron is released into the cells and the iron-free transferrin, also referred to as apotransferrin, is exocytosed outside the cell without being degraded.

Physical form
Solution, 30 mg/ml in IMDM, filtered through 0.2 µm pore size membrane. Iron saturation is below 1%. This product is Apo-Transferrin.
Preparation Note
Working concentration: 1 to 100 µg/ml
Storage and Stability
Store at 2 to 8 °C. (lyophilizate and solution)

differentiation medium
keratinocyte medium
haemogenic endothelium culture medium
embryoid-body medium
blast colony forming cell-culture medium

For life science research only. Not for use in diagnostic procedures.

Quality Level	100
sterility	0.2 µm filtered
form	(clear, red solution)
packaging	pkg of 20 mL (30 mg/ml)
Торговая марка	Roche
application(s)	cell culture \| mammalian: suitable
solubility	water: miscible
UniProt accession no.	P02787,
shipped in	wet ice
storage temp.	2-8°C
Gene Information	human ... TF(7018)

RIDADR	NONH for all modes of transport
WGK Germany	WGK 1
Flash Point F	No data available
Flash Point C	No data available

Transforming Growth Factor-1, human (hTGF-1) 11412272001

Recombinant, human TGF- 1 is produced in CHO (Chinese Hamster Ovary) cells and purified by standard chromatographic techniques.
Solution in PBS and 1 mg/ml BSA, filtered through 0.2 µm pore size membrane.
Specificity
Species specificity: Transforming growth factor-1 (TGF-1) is effective on human and mouse cells.
Specific activity/EC50: <0.1 ng/ml, at least the same specific activity (EC<SUB>50) compared to the indicated standard is guaranteed.

Transforming growth factor-β1, human (hTGF-β1) has been used to explore function and underlying mechanism of periostin (PN) during orthodontic periodontal ligament remodeling.
Biochem/physiol Actions
Transforming growth factor-β (TGF-β) family comprises of a group of multifunctional cytokines which are involved in controlling apoptosis, growth and differentiation of cells, and play important role during embryo development.
Transforming Growth Factor-β1, human (hTGF-β1), is a multifunctional growth factor affecting many functions in a variety of different cells.
Quality
Purity: >95% (SDS-PAGE)
Endotoxin level: <0.1 EU/µg (LAL-test), <10 EU/ml (LAL-test)
(Note: 1 EU corresponds to 0.1 ng)
Sequence
Two identical polypeptide chains (112 amino acids) connected by disulfide bridges, identical to natural hTGF-β1.
Chain Length 2 x 112 AA
Unit Definition
EC50 definition: The concentration of hTGF-1 that is required to mediate half maximal inhibition of DNA synthesis (BrdU incorporation) with Mv1-Lu cells.
Preparation Note
Working concentration: 0.01 - 10 ng/ml
Recombinant, human TGF- 1 exerts its biological activity in the concentration range of 0.01–10 ng/ml.
Working solution: Dilute the concentrated TGF-1 solution (1 µg/ml) with PBS or culture medium containing BSA [or HSA (human serum albumin)], 1 mg/ml (0.1%) or serum 1–10%.
Storage conditions (working solution): For best results, prepare appropriate aliquots and store at -15 to -25 °C.
Note: Avoid repeated freezing and thawing.

For life science research only. Not for use in diagnostic procedures.

Quality Level	100
biological source	human
recombinant	expressed in CHO cells
assay	>95% (SDS-PAGE)
form	solution
potency	<0.1 ng/mL EC₅₀
mol wt	25,000 Da
packaging	pkg of 1 mL (1 µg)
Торговая марка	Roche
storage condition	avoid repeated freeze/thaw cycles
impurities	<0.1 EU/µgtested (LAL test)
UniProt accession no.	P01137,
shipped in	dry ice
storage temp.	20°C
Gene Information	human ... TGFB1(7040)

RIDADR	NONH for all modes of transport
WGK Germany	nwg
Flash Point F	does not flash
Flash Point C	does not flash

Monophasic solution of phenol and guanidine thiocyanate for RNA, DNA, and protein isolation.

TriPure™ Isolation Reagent

Ready-to-use reagent for the simultaneous isolation of total RNA, DNA, and proteins from cells or tissues of human, plant, yeast, bacterial, or viral origin. RNA is undegraded and free of protein or DNA contamination according to the current Quality Control.After purification, many applications are possible:

The DNA-free total RNA is suitable for northern blotting, in vitro translation, RNase protection assays, cDNA synthesis, or RT-PCR.
The RNA-free DNA is suitable for PCR, restriction digestion, Southern blotting, or cloning.
The denatured protein is suitable for SDS-PAGE and western blotting.

Features and Benefits
The TriPure Isolation Reagent allows the simultaneous isolation of RNA, DNA, and protein from the same sample in a single-step liquid-phase separation. RNA, DNA, and protein are separated into different organic and aqueous phases, from which each can be purified by a series of alcohol precipitations.

Work with an easy-to-use kit. The red dye in the reagent simplifies identification of different phases.
Process a wide variety of starting samples. Easily adapt the kit to your specific needs.
Simplify isolation protocols. Use a single reagent that isolates DNA-free RNA, RNA-free DNA, and proteins.
Increase yields of intact RNA. TriPure Isolation Reagent provides an immediate chaotropic denaturing environment that eliminates endogenous RNase activity.

For life science research only. Not for use in diagnostic procedures.

TriPure is a trademark of Roche

form	solution (ready-to-use)
Quality Level	100,
packaging	pkg of 200 mL (11667165001), pkg of 50 mL (11667157001)
Торговая марка	Roche
shipped in	ambient
storage temp.	2-8°C

Tris hydrochloride 10812846001

Empirical Formula (Hill Notation):	C₄H₁₁NO₃ · HCl
Linear Formula:	NH₂C(CH₂OH)₃ · HCl
CAS Number:	1185-53-1
Molecular Weight:	157.60
Beilstein/REAXYS Number:	3675235
MDL number:	MFCD00012590
PubChem Substance ID:	329749168

The pH values of all buffers are temperature and concentration dependent. For Tris buffers, pH increases about 0.03 unit per °C decrease in temperature, and decreases 0.03-0.05 unit per ten-fold dilution.
For precise applications, use a carefully calibrated pH meter with a glass/calomel combination electrode.
Buffering agent in incubation mixtures. It has also been used as a component of lysis and TE (Tris-EDTA) buffer.
Features and Benefits
Crystals
Quality
Purity: >99% Tris-HCl (titrimetric)
Heavy metals: <1 ppm Pb and Fe

For life science research only. Not for use in diagnostic procedures.

Trizma is a registered trademark of Sigma-Aldrich Co. LLC

assay	>99% (titration)
form	solid
packaging	pkg of 500 g
Торговая марка	Roche
pH range	7.0 - 9.0
useful pH range	7.0 - 9.0
pKa (25 °C)	8.1
absorption	<0.02 at 300 nm at 100 mg/mL
shipped in	ambient
storage temp.	room temp
SMILES string	Cl.NC(CO)(CO)CO
InChI	1S/C4H11NO3.ClH/c5-4(1-6,2-7)3-8;/h6-8H,1-3,5H2;1H
InChI key	QKNYBSVHEMOAJP-UHFFFAOYSA-N

Transfer RNAs (tRNA) are responsible for amino acid transport and the correct reading frame in protein biosynthesis. The knowledge of their tertiary structure and interactions with proteins and ribosomes is important for the understanding of mechanisms involved in protein biosynthesis.

RIDADR	NONH for all modes of transport
WGK Germany	WGK 1
Flash Point F	Not applicable
Flash Point C	Not applicable

tRNA

tRNA is added as a competitor to pre- and hybridization solutions to prevent nonspecific binding of the probe.
Quality
This product is tested for the absence of RNase according to the current Quality Control procedures. 1mg of dry substance corresponds to 16A260 units.

For life science research only. Not for use in diagnostic procedures.

Quality Level	100,
form	lyophilized
packaging	pkg of 100 mg (10109541001), pkg of 500 mg (10109550001)
Торговая марка	Roche
shipped in	dry ice
storage temp.	20°C

Trypsin Inhibitor 10109886001

Soybean trypsin inhibitor (STI) comprises 181 amino acids. It is a monomeric protein corresponding to a molecular weight of 20 kDa and has two disulfide bridges. It belongs to serpins − serine protease inhibitors family.
Specificity
Soybean trypsin inhibitor is an inhibitor for trypsin, plasmin, and plasma kallikrein. It inhibits trypsin, factor Xa, plasmin, and plasma kallikrein activity in serum-free cell culture media. It does not inhibit metallo-, cysteine, aspartic proteases, or tissue kallikrein (serine proteases).

Trypsin Inhibitor has been used:

in the buffer for hepatocyte isolation
to inhibit trypsin in Corneal epithelial cells
to inhibit papain activity while treating hippocampal neural stem cells (NSCs)

Trypsin Inhibitor from soybean is used to terminate tissue disaggregation and for subcultivation procedures.
Biochem/physiol Actions
Soybean trypsin inhibitor (STI) inhibits myc proto-oncogene protein and is anticarcinogenic. It favors anti-aggregation of platelets and may be a potential protease inhibiting drug. STI inhibits renin and angiotensin.
Soybean trypsin inhibitor is an inhibitor for trypsin, plasmin, and plasma kallikrein. The product is sensitive to heat, alkaline pH, and protein-precipitating compounds.
Specifications
Inhibiting activity: approximately 70 trypsin inhibitor units/mg lyophilizate at +25°C with benzoyl-L-arginine ethylester as a substrate (approximately 190 trypsin inhibitor units/mg at +25°C with Chromozym TRY as substrate)
Isoelectric point: 4.5
Unit Definition
1 U = 270 S & T-units or 90 USP-units
Preparation Note
Working concentration: 10 to 100 µg/ml
Working solution: Recommended solvent is distilled water.
Stock solution: 1 mg/ml
Storage conditions (working solution): -15 to -25 °C
The enzyme is stable for 6 months, frozen in aliquots.
Reconstitution
Sensitive to heat, alkaline pH, and protein-precipitating compounds.
Storage and Stability
Store at 2 to 8 °C. (Store dry!)

For life science research only. Not for use in diagnostic procedures.

biological source	soybean
Quality Level	100,
form	lyophilized
mol wt	M_r 20,100
packaging	pkg of 50 mg
Торговая марка	Roche
concentration	1 mg/mL
application(s)	cell culture \| mammalian: suitable
pH	3.8-4.5
solubility	water: soluble
shipped in	wet ice
storage temp.	2-8°C

RIDADR	NONH for all modes of transport
WGK Germany	WGK 2
Flash Point F	Not applicable
Flash Point C	Not applicable

Trypsin Inhibitor 10109878001

Egg white trypsin inhibitor is an inhibitor for trypsin, plasmin and plasma kallikrein activity in serum-free cell-culture media. It does not inhibit metallo-, cysteine, and aspartic proteases or tissue kallikrein (serine protease).

Trypsin Inhibitor has been used:

as a component of lysis buffer to treat Tsc2fl/fl (control) and Tsc2fl/flLyz2-Cre (knockout [KO]) bone marrow-derived macrophages (BMDMs) before immunoblotting
to inactivate trypsin post detachment of the stem cells in ventricular zone cell culture
to neutralize trypsin post dissociation and trypsinization of brain tissues
termination of tissue disaggregation and for subcultivation procedures

Chicken egg Trypsin Inhibitor is used for the termination of tissue disaggregation and for subcultivation procedures.
Preparation Note
Working concentration: 0
Working solution: Solvent is recommended in distilled water.
Stock solution: 1 mg/ml
Storage conditions (working solution): -15 to -25 °C
Stable for at least 6 months in distilled water or 1 mM HCI when stored frozen in aliquots. Avoid repeated freeze-thaw cycles.
Reconstitution
Both are soluble in water. Recommended stock solution: 1 mg/ml. Store frozen in aliquots at -15 to -25 °C. Stable for at least 6 months.
Storage and Stability
Store at 2 to 8 °C. (Store dry!)

For life science research only. Not for use in diagnostic procedures.

biological source	chicken egg white
Quality Level	100,
form	powder
packaging	pkg of 1 g
Торговая марка	Roche
concentration	1 mg/mL
application(s)	cell culture \| mammalian: suitable
optimum pH	3.8-4.5
solubility	water: soluble
shipped in	wet ice
storage temp.	2-8°C

RIDADR	NONH for all modes of transport
WGK Germany	WGK 2
Flash Point F	Not applicable
Flash Point C	Not applicable

Trypsin recombinant, Proteomics Grade

3.4.21.4 ( BRENDA | IUBMB )

This trypsin preparation is generated from the recombinant Pichia pastoris strain and is, thus, free of chymotrypsin. Trypsin recombinant, Proteomics Grade, exhibits high specific activity.
Specificity
Serine endopeptidase, hydrolyzing specifically proteins and peptides at the carboxy side of the basic amino acids Arg and Lys. Amide and ester bonds of Arg and Lys are also cleaved.

Trypsin recombinant, Proteomics Grade, is used to specifically digest proteins separated by 2D gel electrophoresis or liquid chromatographic methods during sample preparation for mass spectrometry.
Preparation Note
Stabilizers: Ca2+ in mM concentration range
Inhibitors: TLCK, DFP, PMSF, leupeptin, soybean trypsin inhibitor, trypsin inhibitor from hen egg, aprotinin, 2-macroglobulin, 1-antitrypsin, APMSF, and antipain.
Storage conditions (working solution): -15 to -25°C
The reconstituted solution is stable for 1 month at -15 to -25°C. Avoid repeated freezing/thawing!
Reconstitution
Following reconstitution in 10 mM HCl, Trypsin, recombinant, proteomics grade is stable at -15 to -25 °C for up to one month. After first reconstitution the product must be stored in appropriate aliquots to avoid repeated freezing and thawing.

For life science research only. Not for use in diagnostic procedures.

Quality Level	100,
assay	95% (gel filtration)
form	lyophilized
specific activity	150 units/mg protein
packaging	pkg of 4 x 100 µg (03708969001), pkg of 4 x 25 µg (03708985001)
Торговая марка	Roche
shipped in	dry ice
storage temp.	20°C

Trypsin Sequencing Grade

3.4.21.4 ( BRENDA | IUBMB )

Trypsin Sequencing Grade is isolated from bovine pancreas as a highly purified and specific protease. Trypsin Sequencing Grade is a serine endopeptidase. It specifically cleaves peptide bonds at the carboxylic side of the basic amino acids Arg and Lys. Amide and ester bonds of Arg and Lys are also cleaved.
Specificity
The specificity of Trypsin Sequencing Grade is verified with the oxidized B-chain of insulin (insulin Box) as substrate. High concentrations of Trypsin Sequencing Grade (1 part by weight enzyme with 18 parts by weight insulin Box) are incubated for 18 hours to detect traces of chymotrypsin impurities.
Specificity (HPLC, with Insulin Box):
Cleavage after 1 hour: 90%;
Unspecific cleavage products after 18 hours: 10%

Trypsin Sequencing Grade is used to to digest proteins in solution, in gels or on blotting membranes.
The enzyme is used for protein-structure elucidation, tryptic mapping, fingerprinting, sequence analysis, and translocation studies. Trypsin Sequencing Grade generates glycopeptides from purified glycoproteins and is suited for the digestion of proteins in polyacrylamide gels.
Quality
Purity: Free of impurities that may interfere with the separation of peptides in reversed-phase HPLC.
Preparation Note
Stabilizers: Trypsin is stable in 4 M.
Working concentration: 1/100 to 1/20 of the protein by weight (in solution); 1-5 µg/100 µl (for in-gel digest)
Storage conditions (working solution): A solution in 0.01% trifluoroacetic acid (TFA), (v/v) or 1 mM HCl may be used for one week at maximum, if stored at 2 to 8 °C. By incubation of proteins in solution at neutral to slightly basic pH-values partial autolysis might occur. For this application, Roche recommends Trypsin, Modified, Sequencing Grade.
Reconstitution
Reconstitution in acid is necessary for stability of solution: 0.01% TFA (v/v), 1 mM HCl or 0.1% acetic acid are recommended.

For life science research only. Not for use in diagnostic procedures.

Quality Level	100,
form	lyophilized (salt-free)
specific activity	80 units/mg protein
mol wt	M_r 23.5 kDa
packaging	pkg of 4 x 100 µg (11047841001), pkg of 4 x 25 µg (11418475001)
Торговая марка	Roche
optimum pH	8.0
shipped in	wet ice
storage temp.	2-8°C

Tumor Necrosis Factor-, human (hTNF-) 11371843001

Recombinant tumor necrosis factor-, human (hTNF-), is produced in E. coli and purified by standard chromatographic techniques. Its primary structure is composed of one polypeptide chain (158 amino acids), identical to natural hTNF- (157 amino acids) but with an extra methionine at the amino-terminus.
The TNFA (tumor necrosis factor ) gene is mapped to human chromosome 6p21.33 and codes for a pro-inflammatory cytokine.
Specificity
Human TNF- is effective on mouse and human cells.
Human TNF-a is produced by activated monocytes and macrophages. Human TNF-a has been highly purified and found to have a molecular weight of 17,000 Da (SDS-PAGE). Under nondenaturing conditions, hTNF-a has a molecular weight of approximately 45,000 Da, suggesting that the native protein associates in an oligomeric form.
hTNF-a causes selective necrosis of murine tumors when injected into tumor bearing mice. In vitro hTNF-a has direct cytolytic or cytostatic activity on certain transformed cells. In this context it acts synergistically with interferon-.
Cytotoxicity of hTNF-a for tumor cells has been reported since the initial description of this factor. It has been recognized that hTNF-a also has important effects on several types of normal cells and may have profound effects on inflammatory reactions, bone resorption, the development and function of granulocytes, hemostasis and lipid metabolism (in this context hTNF-a is also known as cachectin). It has also potent antiviral activity in vitro.

Human TNF- (tumor necrosis factor ) is produced by activated monocytes and macrophages.
hTNF- causes selective necrosis of murine tumors when injected into tumor-bearing mice. In vitro, hTNF- has direct cytolytic or cytostatic activity on certain transformed cells. In this context, it acts synergistically with interferon-. hTNF- also has activating and growth stimulating activities on a variety of normal cells and has antiviral enhancing activity on many cell types in vitro. It has been reported in research studies that in vivo hTNF- can cause the necrosis of certain tumors.
Tumor Necrosis Factor-, human (hTNF-) has been used to study the role of ZnO in the regulation of inflammatory responses of vascular endothelial cells via NF-B (nuclear factor-B) signaling. It has also been used to study the its role as a regulator of perlecan production in prostate cancer cells. The TNFA gene is significantly associated with the regulation of innate and adaptive immune responses. Polymorphism of TNFA gene is known to cause acute motor axonal neuropathy. The cytokine release and gene action is associated with epithelial cells, myeloid cells, endothelial, as well as tumor cells. Tumor cells are known to release TNFA, specifically in response to chemotherapy.
Features and Benefits
Growth Enhancement
CCD-18Co (normal human colon)
Detroit 551 (normal human fetal skin)
FS-4 (normal human foreskin)
FS-48 (normal human foreskin)
LL24 (normal human lung)
NRK-49F (normal rat kidney)
Osteoclasts
WI138 (normal human fetal lung)
WI-1003 (normal human lung)

Null response
A549 (human lung carcinoma)
B16 (murine melanoma)
B16F10 (murine melanoma)
Calu-3 (human lung carcinoma)
CMT-93 (murine rectal carcinoma)
G-361 (human melanoma)
HeLa (human cervical carcinoma)
HeLa D98 (human cervical carcinoma)
HT-29 (human colon carcinoma)
HT1080 (human fibrosarcoma)
KB (human oral epidermoid carcinoma)
LS174T (human colon carcinoma)
RD (human rhabdosarcoma)
Saos-2 (human osteogenic sarcoma)
SK-CO-1 (human colon carcinoma)
SK-LU-1 (human lung carcinoma)
SK-OV-3 (human ovarian carcinoma)
SK-UT-1 (human uterine carcinoma)
S49 (murine lymphoma)
T24 (human bladder carcinoma)
WI138 VA 13 (human transformed W138)
Antiproliferative response
BT-20 (human breast carcinoma)
BT-475 (human breast carcinoma)
B6MS2 (murine sarcoma)
B6MS5 (murine sarcoma)
CMS4 (murine sarcoma)
CMS16 (murine sarcoma)
L929 (murine fibroblast)
MCF7 (human breast carcinoma)
ME-180 (human cervical carcinoma)
Meth A (murine sarcoma)
MMT (murine breast carcinoma)
SAC (Moloney-transformed murine 3T3)
SK-MEL-109 (human melanoma)
SK-OV-4 (human ovarian carcinoma)
UV1591-RE (murine fibrosarcoma)
WEHI-164 (murine sarcoma)
WiDr (human colon carcinoma)
Sequence
One polypeptide chain (158 amino acids), identical to natural hTNF-α (157 amino acids), however, it has an extra methionine at the amino-terminus.
Chain Length 158 AA
Unit Definition
EC50 definition: The amount of hTNF- that is required to mediate half-maximal cytotoxicity (MTT cleavage) with WEHI 164 cells in the presence of actinomycin D (1 unit equals 0.01 ng/ml).
Physical form
10 μg/ml solution in PBS and 1 mg/ml BSA, filtered through a 0.2 μm pore size membrane.
Preparation Note
Working concentration: 1 ng/ml
For complete cell lysis of sensitive cell lines about 1 ng/ml is recommended.
Working solution: Dilute the concentrated hTNF- solution (10 µg/ml) with PBS or culture medium containing BSA (or HSA), 1 mg/ml (0.1%) or serum 1-10%.
Storage conditions (working solution): -15 to -25 °C
The solution ca be stored in aliquots at -15 to -25 °C.

For life science research only. Not for use in diagnostic procedures. The biological activity of this product may vary in different in vitro applications. We recommend to determine the optimal concentration range for specific applications.

Quality Level	100
biological source	human
recombinant	expressed in E. coli
assay	>98% (SDS-PAGE)
form	solution
potency	0.01 ng/mL EC₅₀
specific activity	1.0*10^8 U/mg
mol wt	17000 Da
packaging	pkg of 1,000,000 U (10 µg, 1 ml)
Торговая марка	Roche
storage condition	avoid repeated freeze/thaw cycles
impurities	<0.1 EU/µgtested (LAL test)
UniProt accession no.	Q9UBM5,
shipped in	dry ice
storage temp.	20°C
Gene Information	human ... TNF(7124)

RIDADR	NONH for all modes of transport
WGK Germany	nwg
Flash Point F	does not flash
Flash Point C	does not flash

Tumor Necrosis Factor-, mouse (mTNF-) 11271156001

Recombinant murine TNF- is produced in E. coli and purified by standard chromatographic techniques.
Contents:
5 µg/ml solution in PBS and 1 mg/ml BSA, filtered through a 0.2 µm pore size membrane
Specificity
Mouse mTNF- is effective on mouse, rat, rabbit, and human cells.
Specific activity/EC50: >4 x 108 U/mg, <0.0025 ng/ml (mTNF-a, NIBSC, interim standard, 88/532), at least the same specific activity (EC50) compared to the indicated standard is guaranteed.

TNF- causes selective necrosis of murine tumors when injected into tumor-bearing mice. In vitro, human TNF- has direct cytolytic or cytostatic activity on certain transformed cells. In this context, it acts synergistically with interferon-. It has also been used for cell stimulation studies.
Quality
Purity: >95% (SDS-PAGE)
Endotoxin level: <0.1 EU/µg (LAL-test), <10 EU/ml (LAL-test)
Note: 1 EU corresponds to 0.1 ng
Specifications
Primary structure: One polypeptide chain (156 amino acids) identical to natural mTNF-a, but not glycosylated. Glycosylation is not essential for biological activity.
Sequence
Chain Length 156 AA
One polypeptide chain (156 amino acids) identical to natural mTNF-α, but not glycosylated. Glycosylation is not essential for biological activity.
Unit Definition
EC50 definition: The amount of mTNF- that is required to mediate half-maximal cytotoxicity (MTT cleavage) with WEHI 164 cells in the presence of actinomycin D (1 unit equals 0.0025 ng/ml).
Preparation Note
Storage conditions (working solution): -15 to -25 °C
The solution can be stored in aliquots at -15 to -25 °C.
Note: Avoid repeated freezing and thawing.

For life science research only. Not for use in diagnostic procedures.

Quality Level	100
biological source	mouse
recombinant	expressed in E. coli
assay	>95% (SDS-PAGE)
form	solution
potency	<0.0025 ng/mL EC₅₀
mol wt	17,200 Da
packaging	pkg of 2,000,000 U (5 µg, 1ml)
Торговая марка	Roche
storage condition	avoid repeated freeze/thaw cycles
impurities	<1 EU/mgtested (LAL test)
UniProt accession no.	Q6TDG3,
shipped in	dry ice
storage temp.	20°C
Gene Information	mouse ... Tnf(21926)

RIDADR	NONH for all modes of transport
WGK Germany	nwg
Flash Point F	No data available
Flash Point C	No data available

TUNEL AP 11772457001

TUNEL AP is an alkaline phosphatase-labeled antibody used for the in situ detection of apoptosis (programmed cell death) with the TUNEL reaction followed by transmission light microscopy.
The tailing reaction using TdT, also named ISEL (in situ end labeling) or TUNEL (TdT-mediated dUTP nick end labeling), has several advantages in comparison to the in situ nick translation (ISNT) using DNA polymerase:

Label intensity of apoptotic cells is higher with TUNEL compared to ISNT, resulting in an increased sensitivity.
Kinetics of nucleotide incorporation is very rapid with TUNEL compared to the ISNT.
TUNEL preferentially labels apoptotic cells compared to necrotic cells.

TUNEL AP is an antibody that is used to convert fluorescence-based TUNEL assays into colorimetric assays suited for light microscopy. The conversion is performed by binding of an anti-fluorescein antibody to FITC-dUTP. The antibody is labeled with alkaline phosphatase (AP). The AP is visualized with a precipitating substrate, such as Fast Red or NBT/BCIP.
Components
Anti-fluorescein antibody, Fab fragment from sheep, conjugated with alkaline phosphatase (AP). Ready-to-use solution.

For life science research only. Not for use in diagnostic procedures.

form	solution
Quality Level	100,
usage	sufficient for 70 tests
packaging	pkg of 3.5 mL
Торговая марка	Roche
shipped in	wet ice
storage temp.	2-8°C

pictograms	GHS07
signalword	Warning
hcodes	H317
pcodes	P261 - P272 - P280 - P333 + P313 - P362 + P364 - P501
RIDADR	NONH for all modes of transport
WGK Germany	WGK 1
Flash Point F	No data available
Flash Point C	No data available

TUNEL Dilution Buffer 11966006001

TUNEL dilution buffer has been used in terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) assays.
Preparation Note
Working concentration: Working concentration of conjugate depends on application and substrate.

The following concentrations should be taken as a guideline:

ELISA: 100 mU/ml
Western blot: 100mU/ml

Storage conditions (working solution): Dilutions of TdT should be prepared immediately before use and should not be stored.
Keep TUNEL reaction mixture on ice until use.

For life science research only. Not for use in diagnostic procedures.

packaging	pkg of 2 x 10 mL
Quality Level	100,
Торговая марка	Roche
shipped in	wet ice
storage temp.	2-8°C

pictograms	GHS08
signalword	Danger
hcodes	H350i - H412
pcodes	P201 - P202 - P273 - P280 - P308 + P313 - P501
RIDADR	UN 1556 6.1 / PGIII
WGK Germany	WGK 2
Flash Point F	does not flash
Flash Point C	does not flash

TUNEL Label Mix 11767291910

The nucleotide-labeling mix (TUNEL Label) contains fluorescein-dUTP and -dNTPs, both needed to perform the TUNEL (terminal deoxynucleotidyl transferase dUTP nick end labeling) reaction for the detection of apoptosis in situ. The nucleotide-labeling mix is used in combination with the TUNEL enzyme to prepare a TUNEL reaction mixture. This reaction mixture is used to label DNA-strand breaks for detecting and quantifying apoptotic cell death at a single-cell level in cells and tissues.

The nucleotide-labeling mix (TUNEL Label) contains fluorescein-dUTP and -dNTPs, both needed to perform the TUNEL reaction for the detection of apoptosis in situ. The nucleotide-labeling mix is used in combination with the TUNEL Enzyme to prepare a TUNEL reaction mixture. This reaction mixture is used to label DNA-strand breaks for detecting and quantifying apoptotic cell death at a single-cell level in cells and tissues.
TUNEL Label Mix has been used for the determination of apoptosis using TUNEL (terminal deoxynucleotidyl transferase dUTP nick end labeling) assay and DNA nick-end labeling by the TUNEL method.
Preparation Note
Working solution: TUNEL Label is used in combination with the TUNEL Enzyme to prepare the TUNEL reaction mixture.
For one test: Mix 45 µl TUNEL Label with 5 µl TUNEL Enzyme prior to use. For negative control use 50 µl/test TUNEL Label only.
Storage conditions (working solution): Note: The TUNEL reaction mixture (45 µl TUNEL Label with 5 µl TUNEL Enzyme for 1 test) should be prepared just before use, and should not be stored. Keep the TUNEL reaction mixture on ice until use.

For life science research only. Not for use in diagnostic procedures.

form	solution
Quality Level	100,
usage	sufficient for 30 tests
packaging	pkg of 3 x 550 μL
Торговая марка	Roche
shipped in	dry ice
storage temp.	−20°C

pictograms	GHS08,GHS09
signalword	Danger
hcodes	H350i - H411
pcodes	P201 - P273 - P280 - P308 + P313 - P391 - P501
RIDADR	UN 1556 6.1 / PGIII
WGK Germany	WGK 3
Flash Point F	does not flash
Flash Point C	does not flash

TUNEL POD 11772465001

TUNEL POD is a peroxidase-labeled antibody used for the in situ detection of apoptosis (programmed cell death) with the TUNEL reaction followed by transmission light microscopy.

TUNEL POD is an antibody that is used to convert fluorescence-based TUNEL assays into colorimetric assays suited for light microscopy. The antibody is labeled with peroxidase (POD). The peroxidase is visualized with a precipitating substrate such as DAB Substrate. In an experimental study TUNEL (terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling) POD has been used to detect apoptosis in the retina.
Components
Anti-fluorescein antibody, Fab fragment from sheep, conjugated with peroxidase (POD). Ready-to-use solution.

For life science research only. Not for use in diagnostic procedures.

form	solution
Quality Level	100,
usage	sufficient for 70 tests
packaging	pkg of 3.5 mL
Торговая марка	Roche
shipped in	wet ice
storage temp.	2-8°C

pictograms	GHS07
signalword	Warning
hcodes	H317
pcodes	P261 - P272 - P280 - P333 + P313 - P362 + P364 - P501
RIDADR	NONH for all modes of transport
WGK Germany	WGK 1
Flash Point F	No data available
Flash Point C	No data available

Universal ProbeLibrary Human G6PD Assay 5046246001

Gene-specific probes and primer for G6PD (glucose-6-phosphate-1-dehydrogenase) for quantification of gene expression levels using dual-color real-time PCR.
Each Universal ProbeLibrary Reference Gene Assay provides a specifically designed 12-mer UPL reference gene probe and the corresponding reference gene-specific primer pair.
Labeled with LightCycler® Yellow 555 at the 5 end and a dark quencher dye near the 3 end, the UPL reference gene probes can be detected using real-time PCR instruments with excitation filters of 470 nm to 530 nm and emission filters of 550 nm to 610 nm. In multiplex assays, a standard FAM or SYBR Green I filter is used as the first channel to detect FAM-labeled UPL probes for the gene of interest, and a longer-wavelength emission filter (usually 560 nm or 568 nm) is used as the second channel to detect UPL reference gene probes.

Use the Universal ProbeLibrary (UPL) Reference Gene Assays

Human ACTB (-actin) Gene Assay ,
Human GAPD (glyceraldehyde-3-phosphate dehydrogenase) Gene Assay ,
Mouse ACTB (-actin) Gene Assay ,
Mouse GAPD (GAPDH, glyceraldehyde-3-phosphate dehydrogenase) Gene Assay ,

to easily quantify expression levels of a human, or mouse gene of interest in relation to an endogenous reference gene in a dual-color assay.
Design multiplex PCR assays for a target gene and a UPL Reference Gene Assay by using the free web-based ProbeFinder software at the Assay Design Center.
When you select the multiplex option online, ProbeFinder will quickly design multiple UPL assays for your gene of interest. At the same time, each assay is subjected to in silico PCR testing to verify that it can be multiplexed with one (or more) of the UPL Reference Gene Assays for the relevant organism.
Features and Benefits

Significantly reduce assay design time and time to result.
Reduce the cost of gene expression analysis by performing dual-color qPCR assays.
Rely on in silico PCR tested assay combinations for optimal specificity.

Components
The Universal ProbeLibrary Human G6PD Gene Assay package contains four vials:
two vials, each containing 100 µL of a 20 µM solution of two prevalidated primers;
two vials, each containing 100 µL of a 10 µM solution of one prevalidated probe.
Quality
All primers and probes of the Universal ProbeLibrary Reference Gene Assays have passed a real-time PCR performance test and are analyzed by anion-exchange HPLC and MALDI-MS to ensure purity and quality.

For life science research only. Not for use in diagnostic procedures.
Universal ProbeLibrary System Performance Data,
Universal ProbeLibrary System User Statements and Application,
Universal ProbeLibrary System Technology,

Quality Level	100,
Торговая марка	Roche
packaging	pkg of 500 x 20 μL reactions

RIDADR	NONH for all modes of transport
Flash Point F	does not flash
Flash Point C	does not flash

Universal Protease Substrate 11734334001

The Universal Protease Substrate provides rapid and highly sensitive detection of trace protease activity, or determination of the effectiveness of protease inhibition. Protease activity releases resorufin-labeled peptides from the patented substrate, resorufin-labeled casein. Resorufin is N-(resorufin-4-carbonyl)-piperidine-4-carbonic acid).The concentration of these labeled peptides in the supernatant is directly related to the proteolytic activity present.

Conveniently detect nanogram quantities of proteolytic activity in less than one hour.
Perform highly sensitive protease detection in a homogeneous assay.

Principle
By treatment with proteases, resorufin-labeled peptides are released from resorufin-labeled casein. They cannot be precipitated by trichloroacetic acid. The concentration of these resorufin-labeled peptides in the supernatant is equivalent to the proteolytic activity present.

Use Universal Protease Substrate as a general substrate for proteases, and to detect trace protease activities, for example, as a contamination in enzyme preparations. It can be measured spectrophotometrically and fluorimetrically in a homogeneous assay.
Quality
Function test: performance-controlled in the assay for proteases.
Preparation Note
Working concentration: Approximately 1 mg/ml
Storage conditions (working solution): -15 to -25 °C
An aqueous solution is stable for several months at -15 to -25° C and for 2 to 3 days at 2 to 8° C. It is recommended to store aqueous solutions in aliquots at -15 to -25° C. Repeated freezing and thawing is possible. At 15 to 25 °C the product is rapidly hydrolyzed in solution.

For life science research only. Not for use in diagnostic procedures.

Quality Level	100,
form	lyophilized
packaging	pkg of 40 mg (40 μmol; 100mM)
Торговая марка	Roche
concentration	1 mg/mL
shipped in	dry ice
storage temp.	−20°C

RIDADR	NONH for all modes of transport
WGK Germany	WGK 2
Flash Point F	Not applicable
Flash Point C	Not applicable

Uracil-DNA Glycosylase 11444646001

Uracil-DNA Glycosylase (UNG) contains the highly active recombinant form of the equally named enzyme found in prokaryotes and eukaryotes. It hydrolyzes uracil-glycosidic bonds in single- or double-stranded DNA, excising uracil and creating alkali-sensitive abasic sites in the DNA. These abasic sites can be hydrolyzed by endonuclease, heat, or alkali treatment. Depending on how the DNA is prepared, Uracil-DNA Glycosylase can be used to achieve general, site-specific, or strand-specific U-DNA cleavage.
Specificity

Uracil-DNA glycosylase hydrolyzes uracil-glycosidic bonds at U-DNA sites in single- and doublestranded DNA, excising uracil and creating alkali sensitive abasic sites in the DNA.
The enzyme is more active on single-stranded DNA than on double-standed DNA.
Activity was also observed on small U-DNA oligonucleotides and on dUMP (Duncan, unpublished observations).
Uracil-DNA glycosylase is inactive on RNA and native, uracil-free DNA.

Heat inactivation: 95 °C for 10 min
Uracil-DNA glycosylase remains partially active (<10%) after an incubation period of 30 minutes at 95 °C.

Uracil-DNA Glycosylase can be used to cleave DNA at any site where a deoxyuridylate residue has been incorporated. U-DNA can be prepared by in vitro methods like PCR. General, site-specific, or strand-specific cleavage can be achieved with uracil-DNA glycosylase, depending on how the U-DNA is prepared. Uracil-DNA Glycosylase can therefore help you to:

Prevent carryover contamination in PCR
Increase the efficiency of site-directed mutagenesis procedures
Label oligonucleotide probes

Quality
Carryover prevention activity is assayed by adding approximately 105dU that contains templates prior to the amplification reaction. After UNG treatment, no amplification products could be detected. The enzyme does not contain any contaminating exo- or endonucleases and is tested for the absence of RNases.
Unit Definition
One unit is defined as the amount of Uracil-DNA Glycosylase necessary to completely degrade 1 µg purified single-stranded uracil containing DNA (bacteriophage M13, grown in E.coli CJ 236 dut-ung-) at +37 °C in 60 minutes.
One Lindahl unit is defined as the amount of enzyme necessary to release of 1 µmol uracil at +37 °C in 1 minute. One Lindahl unit is comparable to 520,000 U based on our unit definition.
Volume Activity: 1 U/µl
Physical form
The enzyme is supplied as 1U/μl solution in storage buffer.

For life science research only. Not for use in diagnostic procedures.

Quality Level	100,
form	solution
packaging	pkg of 100 U
Торговая марка	Roche
shipped in	dry ice
storage temp.	20°C

RIDADR	NONH for all modes of transport
WGK Germany	WGK 1
Flash Point F	No data available
Flash Point C	No data available

Uracil-DNA Glycosylase, heat-labile

3.2.2.15 ( BRENDA | IUBMB )

Uracil-DNA Glycosylase, heat-labile contains the equally named enzyme found in the marine bacterium BMTU 3346. Like the UNG from E. coli it hydrolyzes uracil-glycosidic bonds in single- or double-stranded DNA, excising uracil and creating alkali-sensitive abasic sites in the DNA. These abasic sites can be hydrolyzed by endonuclease, heat, or alkali treatment. Depending on how the DNA is prepared, Uracil-DNA Glycosylase can be used to achieve general, site-specific, or strand-specific U-DNA cleavage. This enzyme shows lower thermostability and is therefore easier to inactivate.
Enzyme Characteristics
The BMTU 3346 enzyme is inactivated more quickly (2 minutes at +95°C) than the corresponding enzyme from E. coli (10 minutes at +95°C). It has also been reported that UNG from E. coli remains partially active, leading to the degradation of the dU-containing PCR product. In contrast, the heat-labile UNG does not degrade dU-PCR products within at least several hours of incubation at +2 to +8°C. Therefore, it is not necessary to freeze the PCR product immediately after amplification or to hold the reaction mixture at -70°C.
Specificity

Uracil-DNA glycosylase hydrolyzes uracil-glycosidic bonds at U-DNA sites in single- and doublestranded DNA, excising uracil and creating alkali sensitive abasic sites in the DNA.
The enzyme is active on both single-stranded DNA and double-standed DNA.
Uracil-DNA glycosylase is inactive on RNA and native, uracil-free DNA.
Since uracil-DNA glycosylase has no metal ion requirements, it is fully active in the presence of EDTA.

Heat inactivation: 95 °C for 2 min

Uracil-DNA glycosylase can be used to cleave DNA at any site where a deoxyuridylate residue has been incorporated. Because of the heat-lability of Uracil-DNA Glycosylase, heat labile the main application of this enzyme is the prevention of carryover contamination in PCR. In contrast to the enzyme from E.coli; using this preparation of UNG it is not necessary to freeze the PCR product immediately after amplification or to hold the reaction mixture at +70 °C.

Important Note: For highly sensitive techniques like real-time PCR we recommend our LightCycler® Uracil-DNA Glycosylase which is optimized for this application.
Features and Benefits

Prevent carryover contamination in PCR.
Increase the efficiency of site-directed mutagenesis procedures.
Label oligonucleotide probes.
Perform faster inactivation than the corresponding enzyme from E. coli due to the lower thermostability of the enzyme.
Obtain no degradation of dU-PCR products within at least several hours of incubation at +2 to +8°C.

Contents
The enzyme is supplied as 1 U/µl solution in storage buffer.
Quality
Function Test: Carryover prevention activity is assayed by adding approximately 105 dU that contains templates prior to the amplification reaction. After UNG treatment, no amplification products could be detected.
The enzyme does not contain any contaminating exo- or endonucleases and is free from RNase activity, according to the current quality control procedures.
Unit Definition
One unit is defined as the amount of Uracil-DNA Glycosylase required to completely degrade 1 µg purified single-stranded uracil-containing DNA (bacteriophage M13, grown in E. coli CJ236 dut-ung-) at +37 °C in 60 minutes.
One Lindahl unit is defined as the amount of enzyme necessary to release 1 mol uracil at +37 °C in 1 minute. One Lindahl unit is comparable to 520 000 units based on our unit definition.
Volume Activity: 1 U/µl

For general laboratory use.

Quality Level	100,
form	solution
packaging	pkg of 100 U (11775367001), pkg of 500 U (11775375001)
Торговая марка	Roche
optimum pH	8.3-8.9
shipped in	dry ice
storage temp.	−20°C

Water, PCR Grade is specially purified, double-distilled, deionized, and autoclaved. The production process ensures that even according to Roche s strict Quality Control procedures the water does not contain detectable amounts of nucleic acid. It is routinely tested in PCR with conventional thermal cyclers and with LightCycler® Instruments.

Water, PCR Grade

This product is specially tested and qualified for use in all PCR or RT-PCR. It can be used in conjunction with all end-point or real-time PCR assays or whenever highest quality water is needed. All of the LightCycler® kits and some of the amplification products — available from Roche Applied Science — contain this Water, PCR Grade.
Quality
Function test: Each lot of Water, PCR Grade is tested in PCR (amplification of a 0.5 kb target from 0.01 ng DNA). When the PCR product is analyzed by gel electrophoresis, a clear, defined band must be seen on the gel.
Absence of nucleases: The water is tested with various nucleic acids that could serve as nuclease substrates. No endonucleases, ribonucleases or nicking activity are detected according to the current Quality procedures.
Preparation Note
Storage conditions (working solution): Store a working solution for a short period of time (e.g. 1 week) at 2 to 8 °C.

For life science research only. Not for use in diagnostic procedures.

form	liquid
Quality Level	100,
packaging	pkg of 100 mL (03315843001 [4 x 25 ml]), pkg of 25 mL (03315932001 [25 x 1 ml]), pkg of 25 mL (03315959001 [1 x 25 ml])
Торговая марка	Roche
shipped in	dry ice
storage temp.	−20°C

Western Blocking Reagent is used as a general blocking agent during western blotting experiments and immunofluorescence staining. The reagent is used in steps such as blocking the membrane, membrane washing steps, and diluting detection antibodies.
Quality
Each lot is function tested (dot blot).
Physical form
The Western Blocking Reagent is a 10x solution that contains 10% purified casein protein in maleic-acid buffer.
Preparation Note
Working solution: PREPARATION OF WORKING SOLUTIONS

Western Blocking Reagent, Solution

Tris buffered saline (TBS), pH 7.5

To 800 ml redist. water add 6.05 g Tris base (50 mM), 8.76 g sodium chloride (150 mM) and adjust the pH to 7.5 with approx. 9.5 ml 1 M hydrochloric acid. Then dilute to 1 l with double-dist. water. TBS is stable for 3 months, when stored at 2 to 8 °C.
Note: Since sodium azide inhibits POD, it must not be used as antimicrobial agent when using POD-conjugates.

TBS-Tween (TBST)

Washing buffer 1: Dissolve 1 ml Tween 20 in 1 l of TBS. TBST is stable for 3 months, when stored at 2 to 8 °C.
Note: 0.1% Tween 20 is suitable for the most applications, but—depending on the membrane and on the antibody used—different detergents (like SDS, Triton X-100 and Nonidet P40 and detergent concentrations from 0.01 to 1% may lead to better results.

Blocking solution (1%)

Dilute 10 ml Western Blocking Reagent (10x conc.) in 90 ml TBS. The Blocking solution can be stored at 2 to 8 °C for 1 month.
Note: Since sodium azide inhibits POD, it must not be used as antimicrobial agent when using POD-conjugates.

Blocking solution (0.5%)

Dilute 50 ml Blocking solution (1%) with 50 ml of TBS.

Antibody solutions

Dilution and incubation solution for all antibodies is 0.5% Blocking reagent in TBS (see above). In order to exploit the full detection potential of the system we recommend to optimize the dilutions of the primary and secondary antibody in dot blot assays in advance. (Start first with 3 to 4 dilutions of primary antibody and a constant concentration of the second antibody. Then choose the most suitable dilution of primary antibody and optimize the concentration of the secondary antibody in the same way.)
Note: The concentration of the blocking reagent is an important parameter for improvement of the signal to noise ratio in Western blots. If high background appears even under optimized antibody concentrations, increase the concentration of the blocking reagent during the antibody incubations and washing steps from 0.5% to 1%. In case of weak signals even with prolonged antibody incubations lower the concentration of blocking reagent during the antibody incubations and washing steps from 0.5% to 0.1%.

For life science research only. Not for use in diagnostic procedures.

form	solution
Quality Level	100,
usage	sufficient for 10 blots (11921673001 [100 cm²]), sufficient for 60 blots (11921681001 [100 cm²])
packaging	pkg of 100 mL (11921673001), pkg of 6 x 100 mL (11921681001)
Торговая марка	Roche
shipped in	wet ice
storage temp.	2-8°C

X-Gal is a chromogenic substrate for β-galactosidase that produces a rich blue color that can easily be detected visually over background. It is soluble in dimethylformamide and methanol. The product is not soluble in water.

X-Gal

Empirical Formula (Hill Notation):	C₁₄H₁₅BrClNO₆
CAS Number:	7240-90-6
Molecular Weight:	408.63
Beilstein/REAXYS Number:	1402009
MDL number:	MFCD00005666
PubChem Substance ID:	329830810

X-Gal has been used for immunohistocytochemistry applications. It is also the substrate of choice for blue-white selection of recombinant bacterial colonies with the lac+ genotype.
X-Gal is a chromogenic substrate for -galactosidase that produces a rich blue color that can easily be detected visually over background. X-Gal is the substrate of choice for blue-white selection of recombinant bacterial colonies with the lac+ genotype.
Quality
Chromatographically homogeneous
Physical form
Crystals, white powder
Preparation Note
Working solution: Stock solution:

20 mg/ml in dimethyl formamide (DMF), clear, colorless solution
A590 nm: 0.01

Storage conditions (working solution): X-gal in solution (i.e., dissolved in DMF 2% (w/v)) is stable for several weeks when stored in the dark at 2 to 8 °C; when the solution is stored at -15 to -25 °C, it is stable for one year.

For life science research only. Not for use in diagnostic procedures.

Quality Level	100,
packaging	pkg of 1 g (10745740001), pkg of 100 mg (03117073001), pkg of 100 mg (11680293001), pkg of 2.5 g (10703729001), pkg of 250 mg (10651745001)
Торговая марка	Roche
solubility	DMF: soluble, methanol: soluble
shipped in	wet ice
storage temp.	2-8°C
SMILES string	OC[C@H]1O[C@@H](Oc2c[nH]c3ccc(Br)c(Cl)c23)[C@H](O)[C@@H](O)[C@H]1O
InChI	1S/C14H15BrClNO6/c15-5-1-2-6-9(10(5)16)7(3-17-6)22-14-13(21)12(20)11(19)8(4-18)23-14/h1-3,8,11-14,17-21H,4H2/t8-,11+,12+,13-,14-/m1/s1
InChI key	OPIFSICVWOWJMJ-AEOCFKNESA-N

X-tremeGENE™ 360 Transfection Reagent is an innovative reagent that forms a complex with DNA or RNA and efficiently delivers the nucleic acids into animal or insect cells. With improved utility, X-tremeGENE™ 360 delivers high efficiency transfection in more cell types with low cytotoxicity.

X-tremeGENE™ 360 Transfection Reagent

X-tremeGENE™ 360 Transfection Reagent is a high performance transfection reagent, free of animal-derived components.

Designed to transfect a broad range of eukaryotic cells, many cell lines not transfected well by other reagents, and hard-to-transfect cell lines, such as asK-562 and HepG2.
Can be successfully used in a variety of applications, such as gene expression analysis using transiently transfected cells, generating of stable cell lines, expression of siRNA for gene knockdown studies, and CRISPR gene-editing tools.
Produces minimal cytotoxicity or changes in morphology when adequate numbers of cells are transfected, eliminating the requirement to change media after adding the transfection complex.
Suitable for transient and stable transfection.
Functions well in the presence or absence of serum.

Features and Benefits
X-tremeGENE™ 360 Transfection Reagent is a high-performing, versatile and reliable solution for hard-to-transfect and common cell types. As a proven and reliable reagent, X-tremeGENE™ 360 allows researchers to avoid guesswork when performing transfection. In addition, X-tremeGENE™ 360 exhibits:

Peak performance in a broad range of cell types
Suitable for multiple applications
Efficient delivery of plasmid DNA, siRNA/miRNA and CRISPR/Cas9 components

Quality
Each lot of X-tremeGENE™ 360 Transfection Reagent is carefully tested following established quality procedures to ensure that the product is consistently performing according to specifications. During quality testing, cells are transfected with a reporter gene vector DNA using X-tremeGENE™ 360 Transfection Reagent (ratio 3:1 µL/µg DNA). Reporter gene activity is monitored via chemiluminescent detection. Using a standard curve, the total amount of recombinant protein is determined per well in order to meet specification.
Physical form
Supplied in 80% ethanol and sterile-filtered through 0.2 µm pore size membrane. Does not contain any ingredients of human or animal origin. Number of Tests: Using the standard procedure, 1 mL of X-tremeGENE™ 360 Transfection Reagent can be used to perform up to 10,000 transfections in 96-well plates.

For life science research only. Not for use in diagnostic procedures.

X-tremeGENE is a trademark of Roche

grade	for molecular biology
form	liquid (aqueous solution)
packaging	pkg of 0.4 mL (08724105001), pkg of 1.0 mL (08724121001), pkg of 5 x 1.0 mL (08724156001)
Торговая марка	Roche
application(s)	transfection: suitable
shipped in	wet ice
storage temp.	20°C

X-tremeGENE 9 DNA Transfection Reagent is a proprietary blend of lipids and other components supplied in 80% ethanol, filtered through 0.2 μm pore size membrane, and packaged in glass vials.

X-tremeGENE™ 9 DNA Transfection Reagent

X-tremeGENE™ 9 DNA Transfection Reagent is a non-liposomal multi-component reagent for experiments involving cellular analysis. Due to its extremely low cytotoxicity, minimal need for optimization, and the ability to provide high transfection efficiency in a wide range of commonly used cell lines even in the presence of serum, it is well suited for applications in all fields of cellular analysis.
X-tremeGENE™ 9 DNA Transfection Reagent is well suited for cellular analysis applications such as:

Expression of recombinant proteins for functional analysis.
Physiological studies of metabolic pathways.
Analysis of regulatory sequences using reporter gene assays.
Gene expression assays.
Cancer research studies.
Target evaluation.

Quality
Each lot of X-tremeGENE™ 9 DNA Transfection Reagent is carefully tested following established quality procedures to ensure that the product is consistently performing according to specifications. During quality testing, cells are transfected with a reporter gene vector DNA using X-tremeGENE™ 9 DNA Transfection Reagent (ratio 3:1 µl/µg DNA). Reporter gene activity is monitored via chemiluminescent detection. Using a standard curve, the total amount of recombinant protein is determined per well in order to meet specification.
Physical form
Supplied in 80% ethanol and sterile-filtered through 0.2 μm pore size membrane.Number of Tests: Using the standard procedure, 1 ml of X-tremeGENE 9 DNA Transfection Reagent can be used to perform up to 6,600 transfections in 96-well plates using 3:1 ratio and up to 10,000 transfections using 2:1 ratio.

Generate physiologically relevant results using a reagent with extremely low cytotoxicity for maximum post-transfection cell viability.
Save time and eliminate multiple handling steps; simply dilute X-tremeGENE 9 DNA Transfection Reagent, incubate with plasmid DNA, and pipet the mixture directly onto your cells (with or without serum).
Avoid time-consuming optimization procedures in commonly used cell lines.

For life science research only. Not for use in diagnostic procedures.

X-tremeGENE is a trademark of Roche

Quality Level	100,
grade	for molecular biology
form	liquid (aqueous solution)
usage	1 mL (suitable for 165 transfections)
packaging	pkg of 0.4 mL (06365779001), pkg of 1.0 mL (06365787001), pkg of 5 x 1.0 mL (06365809001)
Торговая марка	Roche
application(s)	transfection: suitable
shipped in	wet ice
storage temp.	2-8°C

UN1170 - class 3 - PG 2 - Ethanol, solution

Xanthine Oxidase (XOD) 10110434001

1.1.3.22 ( BRENDA | IUBMB )

Xanthine:oxygen oxidoreductase
Xanthine Oxidase (XOD) is a metal flavoprotein. It has FAD, molybdenum and iron in the ratio 2:2:8.

Xanthine Oxidase has been used to study tyrosine nitration.
Xanthine Oxidase (XOD) has been used in the assessment of XOR-mediated NO production from NDHP and assessment of nitrite-derived NO in liver and purified XOR.
Biochem/physiol Actions
Xanthine Oxidase (XOD) exhibits a broad substrate specificity including aldehydes, purines and pteridines. Furthermore, this enzyme reduces oxygen to generate superoxide, hydrogen peroxide and reactive oxygen species (ROS). It also reduces nitrite to yield reactive nitrogen species (RNS), such as peroxynitrite and nitric oxide. Owing to its ability to generate RNS and ROS, XOD might play an important role as an antimicrobial agent in the neonatal gut, thereby complementing endogenous enzyme of the intestinal epithelium.
Quality
Contaminants: <0.005% guanase, NP and uricase, each, <0.05% ADA, <0.05% alkaline phosphatase (4-nitrophenyl phosphate as the substrate)
Note: Chromatographically purified.
Sequence
XOD is a dimer. Each subunit contains 1 atom of molybdenum, 2 iron-sulfur centers (non-heme iron, ferredoxin-type) and 1 molecule of FAD.
Unit Definition
One unit (U) xanthine oxidase will produce 1 µmol of uric acid (E293nm = 12.2 mmol -1 x L x cm-1) from the oxidation of 1 µmol of xanthine in 1 min at 25 °C and pH8.5.
Physical form
Suspension in 3.2 M ammonium sulfate solution, 10 mM EDTA, pH approximately 8
Preparation Note
Activator: O2
Stabilizers: The substance is stabilized by the addition of EDTA; salicylate is not added.

For life science research only. Not for use in diagnostic procedures.

Quality Level	100,
form	suspension
specific activity	~1 units/mg protein (At 25 °C with xanthine as the substrate.)
packaging	pkg of 1 mL (20 U)
Торговая марка	Roche
optimum pH	8.5-9.0
shipped in	wet ice
storage temp.	2-8°C

Xba I recognizes the sequence T*CTAGA and generates fragments with 5-cohesive termini. The enzyme needs at least two nucleotides around the target sequence before it will cut the cleavage site.
Compatible ends
Xba I ends are compatible with fragments generated by Avr I, Nhe I, and Spe I.
Isoschizomers
The enzyme is not known to have isoschizomers.
Methylation sensitivity
Xba I digestion of DNA is inhibited by the dam gene product of E. coli, which methylates the 6N position of adenine in the sequence GATC. The enzyme is also inhibited by 5-methylcytosine or 5-hydroxymethylcytosine at the site (*) indicated on the recognition sequence.
Activity in SuRE/Cut Buffer System
Buffer printed in bold face type is the buffer recommended for optimal activity:
A B L M H
100% 75-100% 75-100% 75-100% 100%
Relative activity in complete PCR mix
Relative activity in PCR mix (Taq DNA Polymerase buffer) is 60%. The PCR mix contained ?DNA, primers, 10 mM Tris-HCl (pH 8.3, +20°C), 50 mM KCl, 1.5 mM MgCl2, 200 ?M dNTPs, 2.5 U Taq DNA polymerase. The mix was subjected to 25 amplification cycles. Activity in reaction buffer of Pwo SuperYield DNA Polymerase PCR Mix is 25%. When supplemented with GC-RICH Solution, activity increases to 100%.
Incubation temperature
+37°C
Number of cleavage sites on different DNAs
Ad2 SV40 ?X174 M13mp7 M13mp18 pBR322 pBR328 pUC18
1 5 0 0 0 1 0 0 1
PFGE tested
Xba I has been tested in Pulsed-Field Gel Electrophoresis (on bacterial chromosomes). For cleavage of genomic DNA (E. coli C 600) embedded in agarose for PFGE analysis, we recommend 10 U enzyme per ?g DNA and approximately 4 hour incubation time.
Ligation and recutting assay
Xba I fragments obtained by complete digestion of 1 ?g pUC18 DNA are ligated with 1 U T4 DNA Ligase in a volume of 10 ?l by incubation for 16 hours at +4°C in 66 mM Tris-HCl, 5 mM MgCl2, 5 mM Dithiothreitol, 1 mM ATP, pH 7.5 (at +20°C) resulting in >90% recovery of pUC18 DNA.
Subsequent re-cutting with Xba I yields >95% of the typical pattern of pUC18 x Xba I fragments.
Specificity
Star Activity
The sequence specificity of Xba I is relaxed at low ionic strength or by addition of glycerol, ethanol or DMSO to the incubation mixture.
Recognition sites: TCTAGA
TCTAGA
Restriction site: TCTAGA
TCTAGA
Heat inactivation: Xba I can be heat inactivated by incubation at 65 °C for 15 minutes (up to 15 U/µg DNA). Higher concentrations of Xba I cannot be heat inactivated completely under these conditions.

RIDADR	NONH for all modes of transport
WGK Germany	WGK 1
Flash Point F	does not flash
Flash Point C	does not flash

Xba I

The restriction enzyme Xba I has been used for the digestion of genomic DNA.
DNA Profile
Number of cleavage sites on different DNAs

: 1
X174: 0
Ad2: 5
M13mp7: 0
pBR322: 0
pBR328: 0
pUC18: 1
SV40: 0

Unit Definition
One unit is the enzyme activity that completely cleaves 1 µg dam– DNA in one hour at +37 °C in a total volume of 50 µl (1x) SuRE/Cut Buffer H.
Analysis Note
Absence of nonspecific endonuclease activities
1µg DNA is incubated for 16 hours in 50 µl SuRE/Cut Buffer H with an excess of Xba I. The number of enzyme units which do not change the enzyme-specific pattern is stated in the certificate of analysis.
Absence of exonuclease activity
Approximately 5 µg [3H] labeled calf thymus DNA are incubated with 3µl Xba I for 4 hours at +37°C in a total volume of 100 µl 50 mM Tris-HCl, 10 mM MgCl2, 1 mM Dithioerythritol, pH approximately 7.5. Under these conditions, no release of radioactivity is detectable, as stated in the certificate of analysis.
SuRE/Cut Buffer System
The buffer in bold is recommended for optimal activity

A: 100%
B: 75-100%
H: 100%
L: 75-100%
M: 75-100%

Activity in PCR buffer: 60%
Relative activity in PCR mix (Taq DNA Polymerase buffer) is 60%. The PCR mix contained DNA, primers, 10 mM Tris-HCl (pH 8.3, 20 °C), 50 mM KCl, 1.5 mM MgCl2, 200 µM dNTPs, 2.5 U Taq DNA polymerase. The mix was subjected to 25 amplification cycles.Activity in reaction buffer of Pwo SuperYield DNA Polymerase PCR Mix is 25%. When supplemented with GC-RICH Solution, activity increases to 100%. Pwo SuperYield DNA Polymerase PCR Mix is not available in U.S.

For life science research only. Not for use in diagnostic procedures.

Quality Level	100,
form	solution
packaging	pkg of 1,000 U (10674257001 [10 U/µl]), pkg of 20,000 U (10674273001 [10 U/µl]), pkg of 20,000 U (11047663001 [40 U/µl]), pkg of 5,000 U (10674265001 [10 U/µl])
Торговая марка	Roche
parameter	37 °C optimum reaction temp.
shipped in	dry ice
storage temp.	20°C

Use this kit for relative quantification of histone-complexed DNA fragments (mono- and oligonucleosomes) out of the cytoplasma of cells after the induction of apoptosis or when released from necrotic cells. Since the assay does not require prelabeling of cells, it can detect internucleosomal degradation of genomic DNA during apoptosis even in cells that do not proliferate in vitro, for example, freshly isolated tumor cells. The antibodies used in the assay are not species-specific, therefore, the kit may be used to assay cells from a wide variety of species.

Cell Death Detection ELISAPLUS

Anti-histone reacts with the histones H1, H2A, H2B, H3, and H4 of various species (e.g., human, mouse, rat, hamster, cow, opossum, Xenopus). Anti-DNA binds to single- and double-stranded DNA. Therefore, the ELISA allows the detection of mono- and oligonucleosomes from various species, and may be applied to measure apoptotic cell death in many different cell systems.

For research use only. Not for use in diagnostic procedures.
The Cell Death Detection ELISAPLUS photometric enzyme immunoassay is used for the quantitative in vitro determination of cytoplasmic histone-associated DNA fragments (mono- and oligonucleosomes) after induced cell death.
The kit contains a stop solution which allows users to terminate the substrate reaction and run the assay under defined conditions, making it suitable for use in high-throughput applications.

1 kit containing 10 components

One-step ELISA
High sensitivity: (5 x 102 cells/ml)
Fast performance: (3 - 4 hours)
Positive control included
No prelabeling of cells necessary
Nonradioactive assay system
No species restriction
Easy handling
Low background
Suppressed human anti-mouse factor
Function tested

Packaging

11774425001 (1 kit containing 10 components)
11920685001 (1 kit containing 10 components)

Specifications

Assay time: 3 - 4 hours
Negative control: Depending on cell culture conditions, each exponentially growing permanent cell culture contains a certain amount of dead cells (typically approximately 3 - 8%). In the immunoassay, these inherent dead cells in the untreated sample (without a cell-death-inducing agent) will cause a certain absorbance value (negative control).
Positive control: A DNA-histone complex serves as a positive control.
Sample material: Cytoplasmic fractions (lysates) of cell lines, cells ex vivo, cell culture supernatants, and serum or plasma

Unit Conversion: 1 mU = 1 x 10-3 OD (1 mU = 0.001 OD).

Working solution: Preparation of Working Solutions
Alongside the ready-to-use solutions supplied with this kit, you will need to prepare the following working solutions:
Note: Use only double-distilled water for reconstitution of lyophilizates.
Anti-Histone Biotin
Reconstitute the lyophilizate in 450 µl double-distilled water for 10 minutes and mix thoroughly.
Use: Component of the Immunoreagent.
Anti-DNA Peroxidase
Reconstitute the lyophilizate in 450 µl double-distilled water for 10 minutes and mix thoroughly.
Use: Component of the Immunoreagent.
Positive Control
Reconstitute the lyophilizate in 450 µl double-distilled water for 10 minutes and mix thoroughly.
Use: ELISA Step 1.
ABTS Tablets
Dependent on the number of samples tested, dissolve 1, 2, or 3 tablets from bottle 7 in 5, 10, or 15 ml Substrate Buffer.
Use: ELISA Step 5.
ABTS Stop Solution
If turbidity or a precipitate is visible, warm to 37 °C with shaking until the solution is clear.
Use: ELISA Step 6.
Storage conditions (working solution): Anti-Histone Biotin: 2 to 8 °C for 2 months
ABTS Tablets: 1 month stored protected from light. Allow to come to 15 to 25 °C before use.
ABTS Stop Solution: 2 to 8 °C until the expiration date printed on the label.
The exact detection limit of dying/dead cells in a particular sample strongly depends on the kinetics of cell death, the cytotoxic agent used, and the amount of affected cells in the total cell population. Using U937/camptothecin (CAM) as a cellular model system for cell death, the immunoassay allows the specific detection of mono- and oligonucleosomes in the cytoplasmic fraction of 125cell equivalents/well.

For life science research only. Not for use in diagnostic procedures.

usage	sufficient for 10 x 96 multiwell tests (11920685001), sufficient for 96 multiwell tests (11774425001)
Quality Level	100
Торговая марка	Roche
shipped in	wet ice
storage temp.	2-8°C

rGFP 11814524001

GFP isolated from jellyfish Aequorea Victoria exhibited spontaneous fluorescence property. It is a novel important marker for gene expression in various heterologous systems. It is stably present in plant cells and shows photobleaching. Molecular cloning of GFP produces a fused protein with fluorescence excitation and emission spectra.

Heat inactivation: Fluorescence will be quenched by reducing reagents, such as DTT or sodiumdithiosulfate, and is completely inhibited by peroxide.
Fluorescence is inhibited by extreme pH conditions (pH < 4 and pH > 11) as well as ethanol content higher than 60%.

Recombinant green fluorescent protein (rGFP) has also been used in indirect enzyme-linked immunosorbent assay.
Recombinant Green Fluorescent Protein (rGFP) is suitable as:

Positive control when detecting GFP fusion proteins by SDS-PAGE.
Positive control when detecting GFP fusion proteins by western blot using Anti-GFP monoclonal antibody.
Standard for experiments involving fluorescence microscopy.

Solution, 1 mg/ml rGFP in 5 mM Tris-HCl, 5 mM EDTA, pH 8.0

Working concentration: Amount of rGFP recommended for:

SDS-PAGE (Coomassie stained): 1 µg
Western blot: 5 ng

Emission max: 509nm
Excitation max: 395nm
For life science research only. Not for use in diagnostic procedures.

Quality Level	100
form	solution
packaging	pkg of 50 µL (1 mg/ml)
Торговая марка	Roche
shipped in	wet ice
storage temp.	2-8°C

RIDADR	NONH for all modes of transport
WGK Germany	WGK 1
Flash Point F	No data available
Flash Point C	No data available

ABTS™ 10102946001

Empirical Formula (Hill Notation):	C₁₈H₂₄N₆O₆S₄
CAS Number:	30931-67-0
Molecular Weight:	548.68
Beilstein/REAXYS Number:	7329461
MDL number:	MFCD00010404
PubChem Substance ID:	329748893

2,2-azino-di-(3-ethylbenzthiazoline sulfonic acid) or ABTS acts a substrate for HRP (horseradish peroxidase) conjugate during enzyme-linked immunosorbent assay (ELISA). It is the most sensitive, and stable substrate when compared to three other substrates namely, 5-aminosalicylic acid (5AS), O-phenylenediamine (OPD), O-tolidine (OT). It also produces the best visual results, where it gives a bluish-green color. ELISA using ABTS is a highly sensitive, specific and reproducible technique.

ABTS (C18H16N4O6S4-(NH4)2) is a peroxidase substrate for ELISA.
2,2′-Azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) is a peroxidase substrate suitable for use in ELISA procedures. This substrate produces a soluble end product that is green in color and can be read spectrophotometrically at 405 nm. The reaction may be stopped with 1% sodium dodecyl sulfate (SDS). Recommended for ELISA (microwell) procedures, not recommended for membrane applications.

Quality

Purity: >98% (absorbance), chromatographically homogeneous

Working concentration: ABTS should be dissolved as follows:

100 mg ABTS in in 100ml 3.25 mM sodium perborate, 39.8 mM citric acid, 60 mM disodium hydrogen phosphate, pH 4.4-4.5 (see also PI of SA-peroxidase). This buffer corresponds to the single reagent ABTS-Buffer, Cat. No. 1204530. The formed product is green and soluble in water. Measurement at 405 nm.
Dilution of ABTS:
ABTS/ buffer solution (9.1 mM ABTS; pH 5.0): 99,9 mg ABTS in 20 ml potassium phosphate buffer (0.1M; pH 5.0).

Storage and Stability

Store at 2 to 8 °C. (It is also possible to store at -15 to -25 °C)

For life science research only. Not for use in diagnostic procedures.

ABTS is a trademark of Roche

assay	>98%
Quality Level	100
form	crystalline
mol wt	548.68
packaging	pkg of 2 g
Торговая марка	Roche
solubility	50 mg/mL
_max	414 nm
shipped in	wet ice
storage temp.	2-8°C
SMILES string	[NH4+].[NH4+].CCN1C(\Sc2cc(ccc12)S([O-])(=O)=O)=N\N=C3/Sc4cc(ccc4N3CC)S([O-])(=O)=O
InChI	1S/C18H18N4O6S4.2H3N/c1-3-21-13-7-5-11(31(23,24)25)9-15(13)29-17(21)19-20-18-22(4-2)14-8-6-12(32(26,27)28)10-16(14)30-18;;/h5-10H,3-4H2,1-2H3,(H,23,24,25)(H,26,27,28);2*1H3/b19-17-,20-18-;;
InChI key	OHDRQQURAXLVGJ-AXMZSLBLSA-N

RIDADR	NONH for all modes of transport
WGK Germany	WGK 1
Flash Point F	Not applicable
Flash Point C	Not applicable

Alkaline Phosphatase

3.1.3.1 ( BRENDA | IUBMB )

Alkaline phosphatase catalyzes the removal of phosphate group from various compounds that are phosphorylated. Alkaline phosphatase from calf intestine hydrolyzes 5′-monophosphate groups from both DNA and RNA. It can also hydrolyze 5′-diphosphate and 5′-triphosphate groups from RNA.

Use this preparation of calf intestinal alkaline phosphatase to remove 5-terminal phosphates from DNA or RNA and immunoprecipitated RNA samples.
Note: The 11097075001 preparation has a high concentration of enzyme (20 U/µl), which is convenient for large-scale experiments. The 10713023001 preparation is a lower concentration (1 U/µl), which is convenient for small-scale experiments.

Sequence

AP is a zinc-containing enzyme with 4 atoms zinc per molecule (Efstradiatis, 1977).

One unit of alkaline phosphatase is the enzyme activity which hydrolyzes 1 mol of 4-nitrophenyl phosphate in 1 minute at +37 °C under assay conditions.
Note: According to Moessner et al. 5 units alkaline phosphatase (+37 °C; diethanolamine buffer) correspond to 1 unit alkaline phosphatase (+25 °C; glycine/NaOH buffer).
Unit Conversion: Approx. 3.6 U (MB grade AP)
[+37 °C, 4-NPP as substrate, diethanolamine as buffer, pH 9.8] = 1 U [+25 °C, 4.NPP as substrate, glycine as buffer, pH 10.5].
Volume Activity: 20 U/µl for the 11097075001 preparation. 1 U/µl for the 10713023001 preparation.

10713023001: Enzyme solution (1 U/µl) in storage buffer, pH 7.6 (20 °C)
11097075001: Enzyme solution (20 U/µl) in storage buffer, pH 7.6 (20 °C)

Working solution: Storage buffer: 25 mM Tris-HCl, 1 mM MgCl2, 0.1 mM ZnCl2, glycerol 50% (v/v), pH 7.6 (4 °C).
Storage conditions (working solution): Dilutions (1 to 5 U/µl) of MB grade AP in the storage buffer are stable for 17 months at 2 to 8 °C.
Higher Dilutions (~0.01 U/µl) should be made fresh daily and kept at 2 to 8 °C.
Preventing self-ligation of vectors during cloning
If a linearized vector lacks a 5 phosphate, it cannot ligate to itself or form concatamers that contain multiple copies of the vector. Thus, the product of the ligation reaction is predominantly recombinant DNA (vector + DNA insert), rather than religated plasmid.
Inactivation: Add 1/10 volume of EGTA to the reaction mix and incubate at +65°C for 10 minutes. To ensure complete inactivation of enzyme, extract the mix with phenol/chloroform/isoamyl alcohol to remove all protein.

For general laboratory use.

Quality Level	100
biological source	bovine (calf) intestine
form	solution
specific activity	2 units/μg protein
packaging	pkg of 1,000 U (10713023001 [1 U/μl]), pkg of 1,000 U (11097075001 [20 U/μl])
Торговая марка	Roche
parameter	37 °C optimum reaction temp.
optimum pH	7.5-9.5
shipped in	wet ice
storage temp.	2-8°C

-Glucuronidase

3.2.1.31 ( BRENDA | IUBMB )

β-D-Glucuronoside glucuronosohydrolase
Glucuronidation is one of the basic principles of metabolism. Many substances presented to the human body undergo metabolic processing that includes conjugation with glucuronic acid by UDP-glucuronosyltransferases (UGTs). This enzyme catalyzes the transfer of a glucuronyl group to many biological and pharmacologically active endogenous and exogenous molecules. Glucuronide is in general, more soluble, less toxic, and more easily excreted by the human body compared to the original molecule. To analyze these drug conjugates that are present in body fluids, such as urine and plasma, deconjugation of the glucuronide is necessary.
Substances used for doping are conjugated with glucuronides, which means that effective doping analysis relies very often on the enzymatic cleavage of conjugated drug molecules by -glucuronidase.
Enzyme Characteristics
The E. coli -glucuronidase enzyme is essentially free of sulfatase activity and is especially efficient in cleaving steroid and benzodiazepine conjugates.
-D-Glucuronoside glucuronosohydrolase
EC 3.2.1.31

Cleaves terminal glucuronic acid which is β-linked to mono-, oligo- or polysaccharides or phenol.

-Glucuronidases have been used extensively in research and analytical laboratories for the enzymatic hydrolysis of steroid -glucuronides. -Glucuronidase is used:

for the hydrolysis of steroid conjugates (glucuronides) in urine (pH 6.0–6.5)
in doping analysis
for the detection of benzodiazepine in small doses.
during sample preparation to cleave off glucuronides prior to GC-MS, HPLC, immunoassays, or other analytical methods.

It has been used for the hydrolysis of plasma enterolactone, testosterone and epitestosterone glucuronide.

Biochem/physiol Actions

Glucuronidation is one of the basic principles of metabolism. Many substances presented to the human body undergo metabolic processing that includes conjugation with glucuronic acid by UDP-glucuronosyltransferases (UGTs). β-Glucuronidase, also known as β-D-glucuronoside glucuronosohydrolase, catalyzes the transfer of a glucuronyl group to many biological and pharmacologically active endogenous and exogenous molecules. Glucuronide is in general, more soluble, less toxic, and more easily excreted by the human body compared to the original molecule. To analyze these drug conjugates that are present in body fluids, such as urine and plasma, deconjugation of the glucuronide is necessary. Enzymatic hydrolysis prior to detection is essential to achieving high sensitivity during analysis. After hydrolysis, the sample may be analyzed by mass spectroscopy, gas chromatography, HPLC, immunoassays, or other analytical methods.

-Glucuronidase from E. coli is highly specific for -glucuronides, and is capable of very quickly hydrolyzing steroid -glucuronides as well as cleaving many other types of glucuronides, such as benzodiazepine, opioid, and cannabinoid. -Glucuronidase is used for the enzymatic hydrolysis of glucuronides in biological fluids, primarily urine. Substances used for doping are conjugated with glucuronides, which means that effective doping analysis relies very often on the enzymatic cleavage of conjugated drug molecules by -glucuronidase.

Perform fast analysis due to the enzymes high specific activity.
Quickly screen for steroids, benzodiazepines, cannabinoids, and opioids.
Save time by developing your procedure without the need to clean up the reaction or buffer the urine.

The international unit of -glucuronidase activity is the enzyme activity that increases the rate of release of 4-nitrophenol from 4-nitrophenyl--D-glucuronide (4NPG) at a temperature of +25 °C and pH 7.0 by 1 µM.
The Fishman unit was previously used. This unit is the release of phenolphthalein from its glucuronide (PPG). It is not possible to measure the relative activities of different preparations for steroid -glucuronides by comparing their activities with respect to PPG. Many preparation do not catalyze the hydrolysis of PPG, 4NPG, or the various steroid -glucuronides in urine equally. The choice of 4NPG as standard substrate is based on the following considerations:

The Michaelis concentrations for the two substrates are similar (KM = 2 x10-4 M for 4 NPG and KM = 6 x10-5 M for PPG), but the corresponding rates of hydrolysis differ:
4NPG is hydrolysed about 5 x as fast as PPG;
For PPG, inhibition by excess substrate occurs; this is not observed using 4NPG.

Solution in 50% glycerol, pH approximately 6.5
(15 ml in one bottle)

The E.coli -glucuronidase enzyme is essentially free of sulfatase activity and is especially efficient in cleaving steroid and benzodiazepine conjugates.
For life science research only. Not for use in diagnostic procedures.

The sale of the Product does not exhaust or grant any rights in third party patents including patents of companies of the F. Hoffmann - La Roche AG group of companies, in particular, for the use of modified antibodies obtained by using the product.

Quality Level	100
form	solution
specific activity	~80 units/mg protein (Glucuronidase at 25 °C, or 140 U/mg at 37 °C, at pH 7 with 4-nitrophenyl--D-glucuronide as substrate; 1 ml -Glucuronidase contains at least 140 U at 37 °C.)
mol wt	M_r ~220 kDa
packaging	pkg of 1 mL (03707580001), pkg of 15 mL (03707601001), pkg of 5 mL (03707598001)
Торговая марка	Roche
parameter	48 °C optimum reaction temp.
optimum pH	6.0-6.5
shipped in	wet ice
storage temp.	2-8°C

β-Glucuronidase/Arylsulfatase from Helix pomatiais is the most widely used enzyme preparation containing sulfatase activity and has a very broad specificity. It is a crude mixture of enzymes and the preparation does not involve any kind of chromatographic separation. This preparation contains both glucuronidase and sulfatase activity. Enzymatic hydrolysis prior to detection is essential for achieving high sensitivity during analysis. After hydrolysis, the sample may be analyzed by mass spectroscopy, gas chromatography, HPLC, or immunoassays. For doping analysis, the sulfatase activity in addition to the glucuronidase activity is essential for the detection of all drug conjugates present in the sample. β-Glucuronidase/Arylsulfatase is also used for the enzymatic hydrolysis of glucuronides and sulfate esters in biological fluids and primarily urine.

-Glucuronidase/Arylsulfatase

-Glucuronidase/Arylsulfatase shows a broad specificity for many kinds of -glucuronides and sulfate esters.
Specificity of -Glucuronidase:
The glycosides that -D-glucuronic acid forms with a variety of compounds containing hydroxyl groups hydrolyze readily in the presence of -glucuronidase.

Such compounds include steroids, such as estriol (Km = 0.42 mM, pH 4.5), androsterone, pregnanediol, tetrahydrocortisone,
phenols, such as phenolphthalein (Km = 0.39 mM), 4-nitro-phenol, 4-methylumbelliferone,
drugs such as chloramphenicol and tetrahydrocannabinols,
and metabolites such as thyroxine and bilirubin.

Polysaccharides that contain -glucuronic acid residues, such as hyaluronic acid, are also hydrolyzed.
-Glucuronidase is highly specific for the carbohydrate part: neither -glucosides nor -glucosiduronic acids are hydrolyzed. However, the nature of the residue linked to the -glucuronic acid residue is hardly important at all.
Specific activity: 5.5 U/ml at +38°C with phenolphthalein--glucuronide as the substrate (4.5 U/ml at +25°C with 4-nitro-phenyl--D-glucuronide as the substrate = 100,000 Fishman units/ml at +38°C with phenolphthalein--glucuronide as the substrate). 1 Fishman unit releases 1 µg phenolphthalein from phenolphthalein--glucuronide in 1 hour at +38°C.
Specificity of Acrylsulfatase:
Sulfate esters of many phenols are hydrolysed in the presence of arylsulfatase. Examples are steroid sulfates such as estronesulfate, 4-nitrophenyl hydrogen sulfate (Km = 1.8 mM, pH 7.3), 4-nitro-pyrocatechol 2-sulfate (Km = 1.25 mM, pH 7.5), and phenolphthalein disulfate.
Specific activity: 2.6 U/ml at +38°C with phenolphthalein disulfate as the substrate (14 U/ml at +25°C with 4-nitrophenyl sulfate as the substrate = 800,000 Roy units/ml at +38°C with 2-hydroxy-5-nitrophenyl sulfate as the substrate). 1 Roy unit releases 1 µg 2-hydroxy-5-nitrophenyl sulfate in 1 hour at +38°C.
Specificity of -Glucuronidase:
The glycosides that -D-glucuronic acid forms with a variety of compounds containing hydroxyl groups hydrolyze readily in the presence of -glucuronidase.

Such compounds include steroids, such as estriol (Km = 0.42 mM, pH 4.5), androsterone, pregnanediol, tetrahydrocortisone,
phenols, such as phenolphthalein (Km = 0.39 mM), 4-nitro-phenol, 4-methylumbelliferone,
drugs such as chloramphenicol and tetrahydrocannabinols,
and metabolites such as thyroxine and bilirubin.

β-Glucuronidase/Arylsulfatase has been used extensively in research and analytic laboratories for the simultaneous enzymatic hydrolysis of steroid β-glucuronides and sulfate esters. The enzyme is used during sample preparation to cleave off glucuronides and sulfate esters prior to GC-MS, HPLC, immunoassays, or other analytical methods, including doping analysis and hydrolysis of steroid conjugates (glucuronides) and sulfate esters in urine and other body fluids.

Glucuronidation is one of the basic principles of metabolism. Most substances presented to the human body undergo metabolic processing that includes conjugation with glucuronic acid by UDP-glucuronosyltransferases (UGTs). This enzyme catalyzes the transfer of a glucuronyl group to many biological and pharmacologically active endogenous and exogenous molecules. Glucuronide is in general more soluble, less toxic, and more easily excreted by the human body compared to the original molecule.
In addition, sulfation of the drug or chemical substance by sulfotransferases in the human body may occur. Sulfation in general, is less predictable than glucuronidation since many isoenzymes of sulfotransferases exist, and there are individual differences in the ratio of glucuronidation versus sulfation of the substance.

Deconjugate and detect both glucuronides and sulfate esters.
Quickly screen for steroids, benzodiazepines, cannabinoids, opioids, and other drugs.

Components

EC 3.1.6.1 & 3.2.1.31

Principle

Glucuronidase:
Standard unit
The standard unit of -glucuronidase activity is the enzyme activity that increases the rate of release of 4-nitrophenol from 4-nitrophenyl -D-glucosiduronic acid at a temperature of +25 °C and pH 4.5 by 1 µM.
Phenolphthalein unit
The phenolphthalein unit of -glucuronidase activity is the enzyme activity that increases the rate of release of phenolphthalein from phenolphthalein -D-glucosiduronic acid at a temperature of +38 °C by 1 µM.
Approx. 4.5 standard units are equivalent to 5.5 phenolphthalein units.
Fishman unit
The Fishman unit of -glucuronidase activity is the enzyme activity that increases the rate of release of phenolphthalein from phenolphthalein -D-glucosiduronic acid at a temperature of +38 °C by 1 µg.
Approx. 1 standard unit is equivalent to 22,000 Fishman units (1 phenolphthalein unit is equivalent to 19,000 Fishman units).
Arylsulfatase:
Standard unit
The standard unit of arylsulfatase activity is the enzyme activity that increases the rate of release of 4-nitrophenol from 4-nitrophenyl sulfate at a temperature of +25 °C and pH 6.2 by 1 µM.
Phenolphthalein unit
The phenolphthalein unit of arylsulfatase activity is the enzyme activity that increases the rate of release of phenolphthalein from phenolphthalein disulfate at a temperature of +38 °C and pH 6.2 by 1 µM.
Approx. 5.4 standard units are equivalent to 1 phenolphthalein unit.
Roy unit
The Roy unit of arylsulfatase activity is the enzyme activity that increases the rate of release of 4-nitropyrocatechol from 2-hydroxy-5-nitrophenyl hydrogen sulfate (4-nitropyrocatechol 2-sulfate) at a temperature of +38 °C and pH 6.2 by 1 µg.
Approx. 1 standard unit is equivalent to 57,000 Roy units (1 phenolphthalein unit is equivalent to 308,000 Roy units).

Endoglycosidase H

3.2.1.96 ( BRENDA | IUBMB )

Endo--N-acetylglucosaminidase H
Endoglycosidase H hydrolyzes N-linked oligosaccarides of glycopeptides/proteins. It cleaves only high mannose structures.

Active on N-linked oligosaccharides of glycopeptides/proteins.
Cleaves only high-mannose structures (n = 2 - 150, x = [Man]1-2, y = H), and hybrid structures (n = 2, x and/or y = AcNeu-Gal-GlcNAc).

Use Endoglycosidase H for the deglycosylation of glycoproteins. Endo H has been used for the analysis of glycosylation of ATP-binding cassette proteins.

Quality

Absence of contaminants: - and -glucosidase, -galactosidase, -mannosidase, -N-acetyl-hexosaminidase, -L-fucosidase, and proteases are not detectable.

One unit enzyme activity hydrolyzes 1 µmol dabsyl-Asn(GlcNAc)2(Man)5 or 0.2 µmol dansyl-Asn (GlcNAc)2(Man)5 in one minute at 37 °C and pH 5.5.
Note: 5 U, using the dabsyl substrate, corresponds to 1 U using the dansyl substrate.

Solution in 50 mM sodium phosphate, 25 mM EDTA, 0.1% Micr-O-protect; (w/v), pH 7

For life science research only. Not for use in diagnostic procedures.

Quality Level	100
assay	90% (SDS-PAGE)
form	solution
specific activity	~40 units/mg protein (at +37°C and pH 5.5 with dabsyl-Asn(GlcNAc)₂(Man)₅ as the substrate)
mol wt	M_r 29 kDa
packaging	pkg of 200 µL (11088726001 [1U]), pkg of 500 µL (11643053001 [2.5 U])
Торговая марка	Roche
optimum pH	5-6
shipped in	wet ice
storage temp.	2-8°C

N-Acetyl--D-Glucosaminidase (NAG) 10875406001

N-acetyl--D-glucosaminidase (NAG) is mainly used in the colorimetric assay for the determination of N-acetyl--D-glucosaminidase in urine. NAG hydrolyzes 3-cresolsulfonphthaleinyl-N-acetyl-D-glucosaminide to release 3-cresolsulfonphthalein, which is measured photometrically at 580nm. It is an intracellular lysosomal enzyme, present in the S3 segment of proximal tubular cells and distal nephron. Presence of NAG in the urine shows an organelle impairment in proximal tubule. Level of NAG rises in individuals over 70 years of age.

N-acetyl--D-glucosaminidase (NAG) has been used for preparing standards for the determination of N-acetyl--D-glucosaminidase in urine in life-science research applications.

Packaging

1 kit containing 3 components

Storage conditions (working solution): Stability of solutions:
Solution II is stable for 1 month when stored at 2 to 8 °C, protected from light.
Solution III is stable for 1 month stored at 2 to 8 °C.
Stability of the sample:
The activity determination of the N-acetyl--D-glucosaminidase (NAG) should be carried out directly after collecting the sample. Turbid urines should be centrifuged and the supernatant decanted. NAG is stable for one week at 2 to 8 °C and for one month when stored at -15 to -25 °C.

Working solution: Preparation of solutions:

Buffer solution
Dissolve the contents of bottle 1 with 55 ml double-distilledwater.
Substrate solution
Dissolve the contents of bottle 2 with 55 ml solution I.
Stop reagent
Dissolve the contents of bottle 3 with 110 ml double-distilled water.

For life science research only. Not for use in diagnostic procedures.

usage	sufficient for ~50 tests
Quality Level	100
Торговая марка	Roche
shipped in	ambient
storage temp.	room temp

pictograms	GHS07,GHS08
signalword	Danger
hcodes	H319 - H360FD
pcodes	P201 - P202 - P280 - P308 + P313 - P337 + P313 - P501
RIDADR	NONH for all modes of transport
WGK Germany	WGK 2
Flash Point F	does not flash
Flash Point C	does not flash

N-Glycosidase F

3.5.1.52 ( BRENDA | IUBMB )

N-Glycosidase F (PNGase F) is a potent enzyme which hydrolyzes at glycosylamine linkage. It also helps in generating a carbohydrate-free peptide and oligosaccharide with di-N-acetylchitobiose unit.
Peptide-N-glycosidase F, Peptide-N4-(acetyl--glucosaminyl)-asparagine amidase

Hydrolyzes all types of N-glycan chains from glycopeptides and glycoproteins unless they carry α1,3-linked core fucose residues present in insect and plant glycoproteins. Free of contaminating proteolytic activities (x = H or sugar[s]) according to current quality control procedures.

Use N-glycosidase F to cleave all types of asparagine-bound N-glycans, provided that the amino group as well as the carboxyl group are present in a peptide linkage, and that the oligosaccharide has the minimum length of the chitobiose core unit. The reaction products are ammonia, aspartic acid (in the peptide chain), and the complete oligosaccharide.
Note: N-Glycosidase F, recombinant is also available as a solution.

One unit is the enzyme activity which hydrolyzes 1 nmol dabsyl fibrin glycopeptide or 0.2 nmol dansyl fetuin glycoprotein within 1 minute at 37 °C and pH 7.8.

Clear, colorless solution after reconstitution

Storage conditions (working solution): 2 to 8 °C
The reconstituted solution is stable at 2 to 8 °C for at least four weeks.

Reconstitution

Dissolving the content in 0.1 ml redist water (100 unit package) or 0.25 ml double-dist. water (250 unit package) respectively, results in a concentration of 100 mM sodium phosphate buffer, 25 mM EDTA, pH 7.2.
Note: N-Glycosidase F, recombinant is also available as solution with 50% glycerol.

For life science research only. Not for use in diagnostic procedures.

Quality Level	100
assay	90% (SDS-PAGE)
form	lyophilized
specific activity	>25000 units/mg protein
packaging	pkg of 100 U (11365185001), pkg of 250 U (11365193001)
Торговая марка	Roche
optimum pH	7.0-8.0
storage temp.	2-8°C

O-Glycosidase 11347101001

3.2.1.97 ( BRENDA | IUBMB )

O-Glycan-peptide hydrolase
O-Glycopeptide endo-D-galactosyl-N-acetyl--galactosamino hydrolase
O-Glycosidase is isolated from the culture filtrate of Diplococcus pneumoniae

Hydrolyzes Gal-(1,3)GalNAc from O-glycans.
The enzyme releases the disaccharide Gal-(1,3) GaINAc from O-glycans, which is bound to serine or threonine as a core unit. Glycoproteins as well as glycopeptides can serve as substrates. Substitution of the disaccharide by sialic acid prevents cleavage.

O-Glycosidase is used to release the Gal-(1,3)-GaINAc unit from O-glycans (glycoproteins or glycopeptides). Bindings to serine as well as to threonine are hydrolyzed. Substituents at the disaccharide (e.g., sialic acid) prevent the hydrolysis and, therefore, have to be removed chemically or enzymatically (e.g., with neuraminidase from Arthrobacter or from Vibrio cholerae).
O-Glycosidase has been used to selectively deglycosylated chondroitin sulfate proteoglycans (CSPGs).
O-Glycosidase has been used in an experimental study done in order to perform comparative analysis of the fibulin protein family. It has also been used in deglycosylation studies, where protein extracts were incubated with O-Glycosidase and neuraminidase, during cell culture experiments.

Principle

Gal-β(1,3)-GaINAc - ↓ - (Ser/Thr) -peptide/protein (O-Glycosidase)

One unit is the enzyme activity which releases 1 μM Gal-GaINAc from Gal-GaINAc-4-nitrophenyl within one minute at 37 °C at pH 5.

Solution in 50 mM Na-phosphate, 0.02%, Micr-O-protect, 350 mM NaCI, pH 7.5, stabilized with BSA (bovine serum albumin [68 kD])

For life science research only. Not for use in diagnostic procedures.

Quality Level	100
form	solution
specific activity	>2.5 units/mg protein
mol wt	M_r ~160 kDa
packaging	pkg of 25 mU
Торговая марка	Roche
optimum pH	6.0-7.6
shipped in	wet ice
storage temp.	2-8°C

pictograms	GHS07
signalword	Warning
hcodes	H317
pcodes	P261 - P272 - P280 - P333 + P313 - P362 + P364 - P501
RIDADR	NONH for all modes of transport
WGK Germany	nwg
Flash Point F	does not flash
Flash Point C	does not flash

DNase I recombinant 4536282001

3.1.21.1 ( BRENDA | IUBMB )

Double-strand-specific endonuclease that requires bivalent cations for maximal activity.
Properties: Double-strand-specific endonuclease that requires bivalent cations for maximal activity.
Activity: 10,000U/bottle according to Kunitz (+25°C; DNA as substrate).
Unit definition: One unit is the enzyme activity that causes an increase in the absorbance of 0.001 per minutes under assay conditions.

DNase I, recombinant, grade I is used for:Eliminating DNA during protein isolation procedures
Analysis of chromatin structure
Eliminating DNA during sample preparation

Contents
Lyophilizate

One unit, according to Kunitz, is the enzyme activity that under assay conditions causes an absorbance increase at 260 nm of 0.001/minute in 1 ml. Volume activity is determined in 0.1 M sodium acetate, 5 mM MgSO4, pH 5.0.
Assay mixture: Calf thymus DNA (100 µg) is incubated with 20 to 50 U DNase I at +25 °C.
The increase in absorbance is measured at 260 nm.
Information Note: These conditions are used for the determination of activity,according to Kunitz, since the Kunitz assay results in high reproducibility and sensitivity. When using this enzyme for normal experimental purposes, Roche recommends using incubation buffers that are appropriate for a given application, e.g., as mentioned in the standard literature (Sambrook et al., Curr. Prot. Mol. Biol., etc.).

Activator: The enzyme requires divalent cations for maximal activity. The specificity of the reaction depends on the nature of the cation used. In the presence of Mg2+ DNase I causes single-stranded nicks in dsDNA, while in the presence of Mn2+ the enzyme produces double-stranded breaks.
Storage conditions (working solution): Long-term Storage of the Dissolved Enzyme
The solvent generally recommended for DNase I is water. When DNase I is reconstituted in water, the solution can be kept for 2 days at 2 to 8 °C and for 1 month at -15 to -20 °C. For best results, prepare appropriate aliquots and avoid repeated freezing and thawing. However, for long-term storage, carefully dissolve DNase I in one of the buffers listed below. In buffer 1, the enzyme will be stable for several weeks. The enzyme will be stable for at least 18 months if it is dissolved in buffer 2, 3, or 4 and stored at the recommended temperatures.
Information note: Do not vortex the enzyme while dissolving!
Buffer 1: 20 mM Tris-HCl, 20 mM MgCl2, 5 mM CaCl2, 0.1 mM dithioerythritol, 0.1 mM EDTA, 50% (v/v) glycerol, pH 8. Store this solution at -15 to-25 °C; it will not freeze at this temperature and will be stable for several weeks.
Buffer 2: 20 mM Tris-HCl, 50 mM NaCl, 1 mM dithioerythritol, 100 µg/mL BSA, 50% glycerol (v/v), pH 7.6. Store this solution at -15 to -25 °C for up to 18 months; it will not freeze at this temperature.
Buffer 3: 20 mM Tris-HCl, 1 mM MgCl2, 50% (w/v) glycerol, pH 7.5. Store this solution at -15 to -25 °C for up to 18 months; it will not freeze at this temperature.
Buffer 4: 20 mM Tris-HCl, 1 mM MgCl2, pH 7.5. Aliquot in appropriate amounts (e.g., 10 µl), freeze the aliquots quickly on dry ice, and store at -60 °C or below for up to 18 months. Thaw only the amount needed for each experiment. Do not refreeze. Discard any leftover thawed solution.

For life science research only. Not for use in diagnostic procedures.

Quality Level	100
form	lyophilized
packaging	pkg of 2 x 10,000 U
Торговая марка	Roche
shipped in	wet ice
storage temp.	2-8°C

pictograms	GHS08
signalword	Danger
hcodes	H317 - H334
pcodes	P261 - P280 - P284 - P304 + P340 - P333 + P313 - P342 + P311
RIDADR	NONH for all modes of transport
WGK Germany	WGK 1
Flash Point F	does not flash
Flash Point C	does not flash

Nuclease S7 10107921001

Nuclease S7 has been used in ribonuclease selection process for ribosome profiling.

Removal of endogenous RNA from in vitro translation systems
RNA sequencing experiments

Biochem/physiol Actions

Nuclease S7 is an endonuclease that mainly cleaves single-stranded substrates. It also cleaves double-stranded DNA or RNA. It cleaves the 5-phosphodiester bonds of RNA and DNA to yield 3-mononucleotides and oligonucleotides. Activity of the enzyme is dependent on Ca2+ and can be completely inactivated by the addition of EDTA.<

One unit releases a sufficient amount of acid-soluble oligonucleotides to produce an increase of 1.0 at A260.

Storage and Stability

Store unopened reagent at 2-8 °C; when diluted to 1 mg/mL, store at -15 to -25 °C.

For life science research only. Not for use in diagnostic procedures.

Quality Level	100
biological source	Staphylococcus aureus
form	lyophilized
specific activity	~15,000 U/mg
packaging	pkg of 15,000 U
Торговая марка	Roche
optimum pH	7.5
shipped in	wet ice

pictograms	GHS07,GHS08
signalword	Danger
hcodes	H315 - H317 - H319 - H334 - H335
pcodes	P261 - P264 - P280 - P284 - P304 + P340 + P312 - P342 + P311
Target Organs	Respiratory system
RIDADR	NONH for all modes of transport
WGK Germany	WGK 1
Flash Point F	does not flash
Flash Point C	does not flash