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Pancreatin from porcine pancreas
CAS Number: 8049-47-6 EC Number: 232-468-9 MDL number: MFCD00131789 NACRES: NA.54
Кат. номер P7545-100G P7545-500G P7545-25G ApplicationPancreatin is a mixture of several digestive enzymes produced by the exocrine cells of the porcine pancreas. It is a broad-spectrum protease composed of amylase, trypsin, lipase, ribonuclease and protease. It is used for in vitro digestibility analysis. Product P7545 has been used to test the sensitivities of cellulolytic bacteria inhibitors.
The enzyme has been used along with amyloglucosidase for the in vitro digestion of starch in food samples. Pancreatin from Sigma has been used for in vitro pepsin-pancreatin digestion assays while estimating of lower gut digestibility using rumen feed residues. It has also been used along with pepsin to simulate in vitro gastric and ileal digestion of raw materials in pigs.Packaging25, 100, 500 g in poly bottleBiochem/physiol ActionsDue to the enzymatic components such as trypsin, amylase and lipase, pancreatin hydrolyzes proteins, starch and fats. Pancreatin will convert not less than 25 times its weight of potato starch into soluble carbohydrates in 5 minutes in water at 40 °C, will digest not less than 25 times its weight of casein in 60 minutes at pH7.5 at 40 °C and will release not less than 2 microequivalents of acid per min per mg pancreatin from olive oil at pH9.0 at 37 °C.
Pancreatin contains enzymatic components including trypsin, amylase and lipase, ribonuclease, and protease, produced by the exocrine cells of the porcine pancreas. This combination of enzymes allows it to hydrolyze proteins, starch and fats. Pancreatin will convert not less than 25 times its weight of potato starch into soluble carbohydrates in 5 minutes in water at 40°C, will digest not less than 25 times its weight of casein in 60 minutes at pH 7.5 at 40°C and will release not less than microequivalents of acid per min per mg pancreatin from olive oil at pH 9.0 at 37°C.Параметрыform powder Quality Level 200 specific activity 8 x USP specifications contains lactose as extender storage temp. −20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H317 - H319 - H334 - H335 pcodes P261 - P264 - P280 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 Target Organs Respiratory system RIDADR NONH for all modes of transport WGK Germany WGK 1 Узнать цену -
PCSK9 human SRP6285-20UG
NACRES: NA.32 General descriptionProprotein convertase subtilisin/kexin type 9 (PCSK9), is an enzyme which in humans is encoded by the PCSK9 gene. This gene encodes a proprotein convertase belonging to the proteinase K subfamily of the secretory subtilase family. This protein plays a major regulatory role in cholesterol homeostasis. PCSK9 binds to the epidermal growth factor-like repeat A (EGF-A) domain of the low-density lipoprotein receptor (LDLR), inducing LDLR degradation. PCSK9 may also have a role in the differentiation of cortical neurons. Mutations in this gene have been associated with a rare form of autosomal dominant familial hypercholesterolemia (HCHOLA3).
Physical form
Sterile filtered through a 0.22 micron filter. Lyophilized from 1 x PBS, pH 7.4. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.
Reconstitution
Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 100 μg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.Параметрыbiological source human recombinant expressed in HEK 293 cells assay 97% (SDS-PAGE) form lyophilized powder mol wt calculated mol wt 75.1 kDa","observed mol wt 20 kDa (DTT-reduced. Protein migrates due to glycosylation and proteolytic digestion.Gln 31 is the predicted N-terminus.)","observed mol wt 62 kDa packaging pkg of 20 µg impurities <1 EU/µg endotoxin (LAL test) conjugate 6-His tagged (C-terminus) UniProt accession no. Q8NBP7, shipped in wet ice storage temp. 20°C Gene Information human ... PCSK9(255738)
Safety InformationRIDADR NONH for all modes of transport WGK Germany WGK 3 Узнать цену -
PCSK9 murine SRP6286-20UG
NACRES: NA.32 General descriptionProprotein convertase subtilisin/kexin type 9 (PCSK9), is an enzyme which in humans is encoded by the PCSK9 gene. This gene encodes a proprotein convertase belonging to the proteinase K subfamily of the secretory subtilase family. This protein plays a major regulatory role in cholesterol homeostasis. PCSK9 binds to the epidermal growth factor-like repeat A (EGF-A) domain of the low-density lipoprotein receptor (LDLR), inducing LDLR degradation. PCSK9 may also have a role in the differentiation of cortical neurons. Mutations in this gene have been associated with a rare form of autosomal dominant familial hypercholesterolemia (HCHOLA3).
Physical form
Sterile filtered through a 0.22 micron filter. Lyophilized from 1 x PBS, pH 7.4. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.
Reconstitution
Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 100 μg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.Параметрыbiological source mouse recombinant expressed in HEK 293 cells assay 97% (SDS-PAGE) form lyophilized powder mol wt calculated mol wt 72 kDa","observed mol wt 20 kDa (DTT-reduced. Protein migrates due to glycosylation. Gln 35 is the predicted N-terminus .)","observed mol wt 64 kDa packaging pkg of 20 µg impurities <1 EU/µg endotoxin (LAL test) conjugate 6-His tagged (N-terminus) UniProt accession no. Q80W65, shipped in wet ice storage temp. 20°C Gene Information mouse ... PCSK9(100102)
Safety InformationRIDADR NONH for all modes of transport WGK Germany WGK 3 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Pepsin 10108057001
Enzyme Commission (EC) Number: 3.4.23.1 ( BRENDA | IUBMB ) General descriptionPepsin is an aspartic endoproteinase isolated from pig gastric mucosa. It is mainly used for the unspecific hydrolysis of proteins and peptides in acidic media. It also provides a limited hydrolysis of native immunoglobulins to yield biologically active fragments.SpecificityAspartic endopeptidase with relatively broad specificity. Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1′ positions.ApplicationPepsin has been used for the digestion of liver tissue obtained from rat.Preparation NoteWorking concentration: 0.05 to 0.5 mg/ml
Storage conditions (working solution): A pepsin solution is stable at 2 to 8 °C, at least for one week, at neutral pH and under germfree conditions. Frozen aliquots of the enzyme solution are expected to be more stable.
A stock solution in 10 mM HCl (5-10 mg/ml) should be stable for at least one week at 2 to 8 °C, too. Storage light protected, tightly closed.
A short (2 minutes) incubation at 40 °C has negligible effect on the activity of lyophilized pepsin or pepsin in solution.Other NotesFor life science research only. Not for use in diagnostic procedures.Параметрыform lyophilized (salt-free) Quality Level 100 specific activity ~2500 units/mg protein (At 37 °C with hemoglobin as the substrate. One unit is the enzyme activity which liberates the amount of Tyr producing an increase in the absorbance of 0.001/minute at 280 nm.) packaging pkg of 1 g Торговая марка Roche optimum pH 1.8-2.2 shipped in wet ice storage temp. 2-8°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - 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 Not applicable Flash Point C Not applicable Узнать цену -
Pepsin from porcine gastric mucosa
CAS Number: 9001-75-6 Enzyme Commission (EC) Number: 3.4.23.1 ( BRENDA | IUBMB ) EC Number: 232-629-3 MDL number: MFCD00081840 eCl@ss: 42010127
Кат. номер P7000-25G P7000-100G P7000-1KG ApplicationPepsin is a peptidase used to digest proteins and is commonly used in the preparation of Fab fragments from antibodies. Pepsin, from porcine gastric mucosa, has been used to hydrolyze dry cervical samples in mice. Product P7000 is provided as a powder and has been used to treat epithelial cells from a single feline mammary carcinoma.
The enzyme from Sigma has been used to simulate in vitro gastric digestion of cooked cod. It has been used to simulate in vitro gastric digestion of cocoa mass and supplemented dietary fiber. It has also been used to increase the fraction of extractable soluble collagen and to lower the immunogenicity of the resulting collagen from bovine dermal tissue.
Pepsin cleavage can be used to produce F(ab)2 fragments of antibodies. 25, 100 g in poly bottle
1 kg in poly bottle
Biochem/physiol Actions
The enzyme does not cleave at valine, alanine, or glycine linkages. Z-L-tyrosyl-L-phenylalanine, Z-L-glutamyl-L-tyrosine, and Z-L-methionyl-L-tyrosine may be used as substrates for pepsin digestion. Pepsin is inhibited by several phenylalanine-containing peptides.
Pepsin hydrolyzes peptide bonds, not amide or ester linkages. Pepsin cleaves peptides with an aromatic acid on either side of the peptide bond. Sulfur-containing amino acids increase susceptibility to hydrolysis when they are close to the peptide bond. Pepsin preferentially cleaves at the carboxyl side of phenylalanine and leucine and at the carboxyl side of glutamic acid residues. Cleaves Phe-Val, Gln-His, Glu-Ala, Ala-Leu, Leu-Tyr, Tyr-Leu, Gly-Phe, Phe-Phe and Phe-Tyr bonds in the chain of insulin
Pepsin is the major proteolytic enzyme produced in the stomach. It digests proteins through the cleavage of interior peptide linkages..
Preferential cleavage: hydrophobic and aromatic residues in P1 and P1′ postitions. Cleaves Phe-Val, Gln-His, Glu-Ala, Ala-Leu, Leu-Tyr, Tyr-Leu, Gly-Phe, Phe-Phe and Phe-Tyr bonds in the β chain of insulin
Unit Definition
One unit will produce a A280 of 0.001 per min at pH2.0 at 37 °C, measured as TCA-soluble products using hemoglobin as substrate. (Final volume = 16ml. Light path = 1cm.)
Analysis Note
Optimum pH is 2-4. Active in 4 M urea and 3 M guanidine HCl. Stable at 60 °C. Pepsin is irreversibly inactivated at pH 8.0 - 8.5.Параметрыform powder Quality Level 200 specific activity 250 units/mg solid mol wt 35 kDa Featured Industry Diagnostic Assay Manufacturing UniProt accession no. P00791, shipped in wet ice storage temp. 2-8°C Gene Information pig ... LOC396892(396892)
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P261 - P264 - P271 - P280 - P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment dust mask type N95 (US),, Eyeshields,, Faceshields,, Gloves, RIDADR NONH for all modes of transport WGK Germany WGK 1 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Pepsin from porcine gastric mucosa 77161-100G
CAS Number: 9001-75-6 Enzyme Commission (EC) Number: 3.4.23.1 ( BRENDA | IUBMB ) EC Number: 232-629-3 MDL number: MFCD00081840 eCl@ss: 42010127 NACRES: NA.54 ApplicationPepsin cleavage can be used to produce F(ab)2 fragments of antibodies. Biochem/physiol Actions
Preferential cleavage: hydrophobic and aromatic residues in P1 and P1′ postitions. Cleaves Phe-Val, Gln-His, Glu-Ala, Ala-Leu, Leu-Tyr, Tyr-Leu, Gly-Phe, Phe-Phe and Phe-Tyr bonds in the β chain of insulin
Analysis Note
Optimum pH is 2-4. Active in 4 M urea and 3 M guanidine HCl. Stable at 60 °C. Pepsin is irreversibly inactivated at pH 8.0 - 8.5.Other NotesSales restrictions may applyПараметрыAgency/Method USP/NF","tested according to Ph. Eur. form powder mol wt 35 kDa UniProt accession no. P00791, storage temp. 2-8°C Gene Information pig ... LOC396892(396892)
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P261 - P264 - P271 - P280 - P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment dust mask type N95 (US),, Eyeshields,, Faceshields,, Gloves, RIDADR NONH for all modes of transport WGK Germany WGK 1 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Pepsin, Porcine Stomach Mucosa
CAS Number: 9001-75-6 Enzyme Commission (EC) Number: 3.4.23.1 ( BRENDA | IUBMB ) MDL number: MFCD00081840
Кат. номер 516360-100GM 516360-2.5GM 516360-500MG 516360-2.5GMCN 516360-500MGCN General descriptionNative pepsin from porcine stomach mucosa. Secreted by the mucosal lining of the stomach. Active under acidic conditions. Catalyzes the hydrolysis of aminoacyl-proline to an amino acid and proline. Inhibitors include aliphatic alcohols, pepstatin A, and pH >6.0.
Native pepsin from porcine stomach mucosa. Active under acidic conditions. Catalyzes the hydrolysis of aminoacyl-proline to an amino acid and proline. Inhibitors include aliphatic alcohols, pepstatin A, and pH >6.0. Has an optimal pH of 2.0-4.0.
Packaging
500 mg in Plastic ampoule
2 g in Plastic ampoule
Warning
Toxicity: Harmful (C)
Unit Definition
One unit is defined as the amount of enzyme that will digest hemoglobin substrates to TCA-soluble products, measured as a change in absorbance at 280 nm of 0.001 per min at 37°C, pH 2.0.
Reconstitution
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.Other NotesBergmeyer, H.V. 1984. Methods of Enzymatic Analysis (3rd ed., vol. 5) p. 232, Academic Press, New York.Legal InformationCALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, GermanyПараметрыstorage conditions -20C Quality Level 100, form lyophilized specific activity 2000 units/mg protein Торговая марка Calbiochem® storage condition OK to freeze, desiccated solubility 10 mM HCl: 0.5 mg/mL shipped in ambient storage temp. 20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P261 - P264 - P271 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 Target Organs Respiratory system WGK Germany WGK 1 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
PepsinAgarose from porcine gastric mucosa
Enzyme Commission (EC) Number: 3.4.23.1 ( BRENDA | IUBMB ) MDL number: MFCD00081840 NACRES: NA.54
Кат. номер P0609-10KU P0609-50KU P0609-25KU General descriptionPepsin is an enzyme found in gastric secretion.ApplicationPepsin-agarose has been used as an immobilization tool to investigate the refolding ability of the pepsin enzyme. It has also been used for the preparation of F(ab′)2 fragments from rabbit IgG.
Used to produce F(ab)2 fragments of antibodies.1
Pepsin immobilized onto agarose beads can be used to digest and then separate out the active peptides of the glycoprotein gliadin.
Packaging
10000, 25000, 50000 units in poly bottle
Biochem/physiol Actions
Preferentially cleaves C-terminal to Phe, Leu and Glu. It does not cleave at Val, Ala or Gly. pH optimum 2-4. Active in 4 M urea and 3 M guanidine HCl. Stable at 60 °C. Pepsin is irreversibly inactivated at pH > 6.
Unit Definition
One unit will produce a A280 of 0.001 per min at pH 2.0 at 37 °C, measured as TCA-soluble products using hemoglobin as substrate. (Final volume = 16 mL. Light path = 1 cm.)
Quantity
One gram solid swells to 5-10ml packed gel.
Physical form
Lyophilized powder stabilized with lactoseПараметрыform lyophilized powder Quality Level 200 specific activity 30 units/mg dry solid mol wt 35 kDa matrix 4% cross-linked beaded agarose UniProt accession no. P00791, storage temp. 20°C Gene Information pig ... LOC396892(396892)
Safety Informationpictograms GHS08 signalword Danger hcodes H334 pcodes P261 - P284 - P304 + P340 - P342 + P311 - P501 Personal Protective Equipment dust mask type N95 (US),, Eyeshields,, Faceshields,, Gloves, RIDADR NONH for all modes of transport WGK Germany WGK 3 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Pepsinogen II from human gastric mucosa
MDL number: MFCD03457959 NACRES: NA.56
Кат. номер P1615-1MG-PW P1615-1MG ApplicationThe ratio between serum levels of pepsinogens I and II can be determined to identify patients with high risk of gastric cancer.
Biochem/physiol Actions
Used as a marker of gastric mucosa status.
Physical form
Liquid, 20 mM Tris-HCl, pH 8.0Параметрыbiological source human gastric mucosa Quality Level 200 form liquid UniProt accession no. P20142, shipped in wet ice storage temp. 2-8°C Gene Information human ... PGC(5225)
Safety InformationRIDADR NONH for all modes of transport Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Prolidase from porcine kidney
CAS Number: 9025-32-5 Enzyme Commission (EC) Number: 3.4.13.9 ( BRENDA | IUBMB ) EC Number: 232-791-5 MDL number: MFCD00132079
Кат. номер P6675-1KU P6675-250UN P6675-100UN P6675-2KU General descriptionProlidase is a cytosolic exopeptidase. It is a homodimeric enzyme which requires divalent cations like manganese as a cofactor in its active site for its function.ApplicationProlidase has an important role in recycling of proline and collagen production. It is used to study mutations in the PEPD gene that cause prolidase deficiency. It is used to hydrolyze proteins with C-terminal proline or hydroxyproline residues. Prolidase, product P6675 from porcine kidney, has been used to hydrolyze peptide bonds from the amino terminus when studying enzymatic methylation of membrane proteins.
Prolidase from porcine kidney has been used:- in the enzymatic hydrolysis of porcine milk for the recovery of L-glutamine from proteins and peptides
- in the proteolysis of skim milk for the determination of -(-glutamyl)lysine and free aminoacids
- to determine its effect on the activity of enterococcin A 2000
Packaging
250, 1000 units in glass bottle
Biochem/physiol Actions
Prolidase is an enzyme that catalyzes the hydrolysis of the imide bond between an α-carboxyl group and proline or hydroxyproline. The protein forms a homodimer that hydrolyzes dipeptides or tripeptides with C-terminal proline or hydroxyproline residues.
Rare mutation in prolidase gene causes deficiency leading to massive imidodipeptiduria, elevated proline-containing dipeptides in plasma, recurrent infections, mental retardation and skin lesions.
Unit Definition
One unit will hydrolyze 1.0 μmole of Gly-Pro per min at pH 8.0 at 40 °C.
Physical form
Supplied as a lyophilized powder containing Tris buffer salt and MnCl2.Параметрыform lyophilized powder Quality Level 200, specific activity ≥100 units/mg protein composition Protein, 20-74% Lowry storage temp. −20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P261 - P264 - P271 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 Target Organs Respiratory system RIDADR NONH for all modes of transport WGK Germany WGK 1 Узнать цену -
Proline Specific Endopeptidase from Flavobacterium sp. E1411-50UN
NACRES: NA.54 ApplicationProline specific endopeptidase is useful for the determination of amino acid sequences of peptides and proteins containing proline residues. Proline specific endopeptidases may be useful in cancer, neurology and diabetes research . Prolyl endopeptidase (PEP) may be used as a drug target for neuropsychiatric diseases such as stress disorder, depression, and schizophrenia .
Packaging
50 units in glass bottle
Biochem/physiol Actions
An endopeptidase is a proteolytic peptidase that breaks peptide bonds of nonterminal amino acids. Product E1411 is specific for proline (Pro). The Prolyl endopeptidase (PEP) mechanism is thought to be an induced fit mechanism, where the native enzyme exists in a conformationally flexible opened state but is changed to a closed state upon substrate binding .
Unit Definition
One unit causes the formation of one micromole of p-nitroaniline per minute under specific pH and temperature conditions.
Physical form
White amorphous lyophilized powderПараметрыform lyophilized powder Quality Level 200, specific activity 5.0 units/mg solid mol wt ~78 kDa shipped in dry ice storage temp. 20°C
Safety InformationRIDADR NONH for all modes of transport WGK Germany WGK 3 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Prolyl oligopeptidase
NACRES: NA.54
Кат. номер O9515-20UG O9515-20UG-PW General descriptionProlyl oligopeptidase (PO) is mapped to human chromosome 6q22. It comprises of a N-terminal β-propeller domain and C-terminal α/β hydrolase catalytic domain. PO is highly expressed in the neuronal cytoplasm and its expression increases with age.
Prolyl oligopeptidase is a cytosolic serine peptidase which cleaves peptide bonds at the C′ terminal side of prolines. It is only capable of processing peptides containing no more than 30 amino acids due to the unique β-propeller region that regulates access to the active site.ApplicationProlyl oligopeptidase has been used in a study to assess the mechanism of lithium ion action. It has also been used in a study to investigate its distribution in human tissue and body fluids.
Prolyl oligopeptidase has been used in the prolyl oligopeptidase inhibitory activity assay in lyophilized protein hydrolysate samples and Schistosoma mansoni samples.
Biochem/physiol Actions
Prolyl oligopeptidase (PO) regulates physiological processes and is crucial for the generation of active hormone and peptide fragments from their precursors. It shows elevated levels in psychiatric disorders and Alzheimer′s patients. Altered levels of PO is observed in patients with bipolar disorder. High expression of PO may promote metastasis of malignant ovarian and colorectal tumors.
Unit Definition
One unit will hydrolyze 1.0 picomole of Ala-Pro-aminomethylcoumarin per minute at pH 7.4 at 25 °C.
Physical form
Supplied as a solution in 45 mM Tris-HCl, pH 8.0, 124 mM NaCl, 2.4 mM KCl, 10% glycerol, 3 mM DTT and variable amounts of imidazole.
Preparation Note
N-terminal GST-tagged 81.6 kDa full-length proteinПараметрыQuality Level 200, recombinant expressed in E. coli assay 90% (SDS-PAGE) form solution specific activity 10 unit/µg protein mol wt 81.6 kDa shipped in dry ice storage temp. 70°C
Safety InformationRIDADR NONH for all modes of transport WGK Germany WGK 1 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Protease from Aspergillus oryzae
EC Number: 232-752-2 MDL number: MFCD00132092 NACRES: NA.54
Кат. номер P6110-50ML P6110-250ML General descriptionFungal protease/peptidase complex produced by submerged fermentation of a selected strain of Aspergillus oryzae and contains both endoprotease and exopeptidase activities.ApplicationThe enzyme from Sigma has been used in the semi-purification of mouse colorectal mucins during protein digestion.
Protease is used to degrade proteins, to study protease inhibitors and to study thermal inactivation kinetics. Protease is used in nucleic acid isolation procedures in incubations. It has been injected into flies with a nanoject apparatus for infection and survival experiments.
Packaging
250 mL in glass bottle
Unit Definition
One unit is the amount of enzyme which hydrolyzes 1 mmol of L-Ieucine-p-nitroanilide per minute.Legal InformationA product of Novozyme Corp.
Flavourzyme is a registered trademark of Novozymes Corp.Параметрыform liquid Quality Level 200, specific activity 500 U/g storage temp. 2-8°C
Safety Informationpictograms GHS05,GHS07,GHS08,GHS09 signalword Danger hcodes H302 - H315 - H318 - H334 - H335 - H410 pcodes P273 - P280 - P301 + P312 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment dust mask type N95 (US),, Eyeshields,, Faceshields,, Gloves, RIDADR UN 3082 9 / PGIII WGK Germany WGK 1 Узнать цену -
Protease from Aspergillus saitoi
CAS Number: 9025-49-4 Enzyme Commission (EC) Number: 3.4.23.18 ( BRENDA | IUBMB ) EC Number: 232-796-2 MDL number: MFCD00132092 eCl@ss: 32160410 NACRES: NA.54
Кат. номер P2143-5G P2143-25G P2143-100G ApplicationProtease from Aspergillus saitoi has been used in a study to assess sequence coverage and resolution in hydrogen exchange of large proteins. It has also been used in a study to investigate the conversion of soybean curd isoflavone glycosides to their aglycones through -glucosidase..
Packaging
5, 25 g in glass bottle
Biochem/physiol Actions
Protease from Aspergillus saitoi was shown to also function as a -glucosidase.
Unit Definition
One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 2.8 at 37 °C (color by Folin-Ciocalteu reagent).Параметрыtype Type XIII Quality Level 200, form solid specific activity 0.6 unit/mg solid foreign activity alkaline protease, essentially free storage temp. 20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system RIDADR NONH for all modes of transport WGK Germany WGK 3 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Protease from Bacillus amyloliquefaciens
EC Number: 232-752-2 MDL number: MFCD00132092 NACRES: NA.54
Кат. номер P1236-250ML P1236-50ML General descriptionBacterial protease produced by submerged fermentation of a selected strain of Bacillus amyloliquefaciensApplicationProtease from Bacillus amyloliquefaciens has been used for the unhairing of hides and skins. It has also been used in a study to investigate peptide bond formation using the carbamoylmethyl ester as the acyl donor.
Packaging
250 mL in glass bottle
Biochem/physiol Actions
Secretion of protease by Bacillus amyloliquefaciens can be inhibited by treatment with the fatty acid synthetase inhibitor cerulenin.Legal InformationA product of Novozyme Corp.
Neutrase is a registered trademark of Novozymes Corp.Параметрыform liquid Quality Level 200, specific activity 0.8 U/g storage temp. 2-8°C
Safety Informationpictograms GHS08 signalword Danger hcodes H334 pcodes P261 - P284 - P304 + P340 + P312 - P501 Personal Protective Equipment dust mask type N95 (US),, Eyeshields,, Faceshields,, Gloves, RIDADR UN 3082 9 / PGIII WGK Germany WGK 3 Узнать цену -
Protease from Bacillus licheniformis
CAS Number: 9014-01-1 Enzyme Commission (EC) Number: 3.4.21.62 ( BRENDA | IUBMB ) EC Number: 232-752-2 MDL number: MFCD00132092 NACRES: NA.54
Кат. номер P5380-1G-C P5380-25MG-C P5380-25MG P5380-1G P5380-250MG P5380-100MG General descriptionThe enzyme is found to be stable at pH 8-10, retaining activity of up to 90% for 24 hours. It shows maximum activity at temperatures between 55-60 °C.SpecificitySubtilisin A is a member of the Serine S8 Endoproteinase family. It has broad specificity with a preference for a large uncharged residue in the P1 position. It hydrolyzes native and denatured proteins, and is active under alkaline conditions.ApplicationThe product has been used with other enzymes for in situ proteolysis to produce crystals suitable for structure determination. It has also been used in the process of isolation of subsarcolemmal (SS) and intermyofibrillar (IMF) mitochondria that can be used for functional in vitro studies.
Non-specific Protease Activity Assay Video
This is a proteolytic enzyme isolated from the fermentation of Bacillus licheniformis. It is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions.Packaging25 mg in poly bottle
1 g in glass bottle
100, 250 mg in glass bottleBiochem/physiol ActionsProtease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Protease, Product P5380, is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. It is active in some organic solvents such as dry octane.Physical propertiesSubtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa.Unit DefinitionOne unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).ПараметрыQuality Level 200 type Type VIII form lyophilized powder specific activity 7-15 units/mg solid mol wt 27 kDa purified by crystallization solubility 10 mM NaAc (pH 7.5) and 5 mM CaAc: soluble, clear, H2O: soluble, colorless foreign activity DNase 5.0 Kunitz units/mg solid, RNase 0.05 Kunitz units/mg solid storage temp. 20°C
Safety Informationpictograms GHS05,GHS07,GHS08,GHS09 signalword Danger hcodes H302 - H315 - H318 - H334 - H335 - H410 pcodes P261 - P273 - P280 - P301 + P312 - P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment dust mask type N95 (US), Eyeshields, Faceshields, Gloves RIDADR UN 3082 9 / PGIII WGK Germany WGK 1 Узнать цену -
Protease from Bacillus sp.
Enzyme Commission (EC) Number: 3.4.21.14 EC Number: 232-909-5 MDL number: MFCD00132092 NACRES: NA.54
Кат. номер P0029-50G P0029-250G General descriptionProtease from Bacillus sp. is extensively useful in pharmaceutical, leather, food and waste processing industry. It is widely used in manufacturing protein hydrolysates. Analysis of Bacillus protease stability and activity showed that the enzyme was active at all pH values from 5.0-11.0 with 100% activity at 8.0. Optimal pH for protein stability was determined to be at 7.0 while the optimal temperature for stability was at 60°C with 95% activity maintained.ApplicationProtease from Bacillus sp. has been used:- to evaluate protease inhibitor activity
- in high yields in batch fermentation using a response surface methodology
- in a study to investigate a biosensor to detect a protease biomarker from Bacillus licheniformis
Packaging
50, 250 g in glass bottle
Analysis Note
minimum activity 1.5 AU-N/G solidLegal InformationProtamex is a registered trademark of Novozymes Corp.Параметрыform granular Quality Level 200, enzyme activity >1.5 AU-N/g storage temp. 2-8°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system RIDADR NONH for all modes of transport WGK Germany WGK 2 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Protease from bovine pancreas
CAS Number: 9001-92-7 EC Number: 232-642-4 MDL number: MFCD00132092 eCl@ss: 32160410 NACRES: NA.54
Кат. номер P4630-250MG P4630-5G P4630-10G P4630-1G ApplicationProtease is an enzyme used to break down proteins by hydrolyzing peptide bonds. Protease is used to degrade proteins, to study protease inhibitors and to study thermal inactivation kinetics. Product P4630 is from bovine pancreas. Protease from bovine pancrease (type I) has been used for the extraction of hemicellulose.
Non-specific Protease Activity Assay Video
Packaging
250 mg in poly bottle
1, 5, 10 g in poly bottle
Biochem/physiol Actions
Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate.
Quality
Crude
Unit Definition
One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent), unless otherwise indicated.Параметрыtype Type I Quality Level 200, form powder specific activity ≥5 units/mg solid storage temp. −20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment dust mask type N95 (US),, Eyeshields,, Faceshields,, Gloves, RIDADR NONH for all modes of transport WGK Germany WGK 1 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Protease from Rhizopus sp. P0107-5G
CAS Number: 9001-92-7 MDL number: MFCD00132092 eCl@ss: 32160410 NACRES: NA.54 General descriptionStable in the acid range of pH 3-5. pH Optimum is 3.0.
Proteases are proteolytic enzymes that digests the proteins. It is classified into acidic, neutral and alkaline proteases based on their pH optimum. Proteases finds its applications in textile industries, laundry and healthcare. It is also being used in food processing industries such as baking and brewing. Rhizopus chinensis is the key species in the production of aspartate proteinase.
Exhibits both proteolytic and lipolytic activities.ApplicationProtease from Rhizopus spp. Has been used in a study to assess the amino acid sequences near the amino termini using automated Edman degradation. It has also been used in a study to investigate inactivation of the enzyme by reaction with diazoacetyl-DL-norleucine methyl ester in the presence of cupric acetate.
Protease from Rhizopus sp. has been used in the enzyme treatment of planted and nonplanted scots pine seedlings.
Packaging
5 g in poly bottle
Biochem/physiol Actions
Protease from Rhizopus chinensis can be inhibited by pepstatin.
Unit Definition
One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 3.0 at 37 °C (color by Folin-Ciocalteu reagent), unless otherwise indicated.
Physical form
Supplied as a powder containing dextrin as a stabilizerПараметрыQuality Level 200, description acidic protease form powder specific activity 0.2 unit/mg solid storage temp. 2-8°C
Safety InformationRIDADR NONH for all modes of transport WGK Germany WGK 3 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Protease from Streptomyces griseus
CAS Number: 9036-06-0 EC Number: 232-909-5 MDL number: MFCD00132092 eCl@ss: 32160410
Кат. номер P5147-1G-C P5147-5G-C P5147-5G P5147-1G P5147-100MG SpecificityA mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.ApplicationProtease from Streptomyces griseus has been used:- for the digestion of nucleus pulposus (NP) tissue
- in the catalysis of asymmetric one pot Mannich reaction
- for deproteinization of starch
- digestion of brain slices for the cell dissociation
Protease is an enzyme used to break down proteins by hydrolyzing peptide bonds. Protease is used to degrade proteins, to study protease inhibitors and to study thermal inactivation kinetics. Protease is used in nucleic acid isolation procedures in incubations. Protease from Streptomyces griseus has been used in crystallographic and kinetic investigations of the covalent complex formed by tetrapeptide aldehydes and serine proteases.
This enzyme is more active at a higher pH range than the known alkaline protease, showing the proteolytic activity even in 0.2N NaOH solution. This enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein.
Protease is typically used in nucleic acid isolation procedures in incubations of 0.5-3.0 hours supplemented with 0.2% sodium dodecyl sulfate and 10 mM EDTA.
The enzyme from Sigma has been used for the digestion and analysis of antithrombin-heparin complexes. It has also been used for the isolation of enzyme-resistant starch.Packaging100 mg in glass bottle
1, 5 g in glass bottleBiochem/physiol ActionsThis product is a mixture of at least three caseinolytic activities and one aminopeptidase activity. The caseinolytic enzymes were named as Streptomyces griseus Protease A, Streptomyces griseus Protease B and Streptomyces griseus Trypsin. This product may be used when extensive or complete degradation of protein is required. This protease mixture is highly nonspecific and can digest casein to the extent of >70% as mono-amino acids.
Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Protease from Streptomyces griseus is a mixture of at least three proteolytic activities including an extracellular serine protease. Serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.Features and Benefits- highly stable in pH range of 5.0 to 9.0, with peak activity at pH 8.8
- compatible with many DNA and RNA isolation buffers
- broad substrate specificity
QualityContains calcium acetate.Physical propertiesCompletely inactivated by heating above 80 °C for 15-20 minutes.Unit DefinitionOne unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).Preparation NoteCollected from culture broth of S. griseus.ПараметрыQuality Level 200 type Type XIV form powder specific activity 3.5 units/mg solid solubility 10 mM NaAc (pH 7.5) and 5 mM CaAc: soluble 0.2 mg/mL at 37 °C, clear, colorless to tan shipped in wet ice storage temp. 20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment Eyeshields, Gloves, type N95 (US) RIDADR NONH for all modes of transport WGK Germany WGK 2 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Protease from Streptomyces sp.
CAS Number: 9036-06-0 EC Number: 232-909-5 MDL number: MFCD00132092 NACRES: NA.54
Кат. номер P0652-500UN P0652-1KU P0652-100UN ApplicationPronase E can be used to degrade antheraea pernyi silk fibroin films.
This enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein. Proteases from Streptomyces griseus and Streptomyces omiyaensis have been used in a study to identify residue 71 as a crucial residue for differences in topological specificities. Proteases have also been used in a study to investigate production of protease as a by-product of streptomycin production.
Protease is typically used in nucleic acid isolation procedures in incubations of 0.5-3.0 hours supplemented with 0.2% sodium dodecyl sulfate and 10 mM EDTA.
Completely inactivated by heating above 80 °C for 15-20 minutes.
A mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.
Packaging
500 units in glass bottle
Biochem/physiol Actions
Alkaline protease that is approximately twice as active at pH 11.0 than at the usual assay conditions for protease, pH 7.5 and 37 °C. By comparison, P5147 Type XIV protease is only approximately 25% as active at pH 11.0, 30 °C.
Physical properties
Isoelectric point : 8.7
Inhibitors : Diisopropyl fluorophosphate, EDTA
Optimum pH : >=12
Optimum temperature : 60oC
pH Stability : pH 5.0 - 11.5 (25oC,24hr)
Thermal stability : below 50oC (pH 8.3, 15min)
Unit Definition
One unit will hydrolyze casein to produce peptide equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 11.0 at 30 °C.
Physical form
This enzyme is more active at a higher pH range than the known alkaline protease, showing the proteolytic activity even in 0.2N NaOH solution. This enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein.
Preparation Note
Collected from culture broth of S.SpПараметрыtype Type XXI Quality Level 200, form powder specific activity 15 units/mg solid mol wt ~50 kDa storage temp. 20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment Eyeshields,, Gloves,, type N95 (US), RIDADR NONH for all modes of transport WGK Germany WGK 2 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Proteinase 3 from human leukocytes
Enzyme Commission (EC) Number: 3.4.21.76 ( BRENDA | IUBMB ) MDL number: MFCD03458212 NACRES: NA.54
Кат. номер E3539-100UG E3539-200UG General descriptionProteinase 3 is found in high concentration in the primary granules of myeloid leukemia blasts.4ApplicationProteinase 3 has been shown to be important in the pathogenesis of human emphysema.1 It has also been used in a study to investigate the liberation of the antibacterial and cytotoxic peptide LL-37 by cleavage of human cathelicidin hCAP-183.2
Biochem/physiol Actions
Used for the detection of anti-PR3 auto-antibodies in immunoassays.
Proteinase 3 (PR-3) is a serine protease expressed in the granules of neutrophils and monocytes. Also known as myeloblastin and p29b, it degrades elastin and is associated with myeloid leukemia and Wegeners granulomatosis.3
Physical form
Solution in 50 mM sodium acetate (pH 5) with 600 mM sodium chlorideПараметрыQuality Level 200 assay 95% (PAGE) form buffered aqueous solution UniProt accession no. P24158, storage temp. 20°C Gene Information human ... PRTN3(5657)
Safety InformationRIDADR NONH for all modes of transport WGK Germany WGK 1 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Proteinase 3 from human neutrophils SRP6309-25UG
General descriptionProteinase 3 is one of the serine proteinases localized in azurophil granules of polymorphonuclear leukocytes. It has been identified as the autoantigen of Wegener granulomatosis, a systemic vasculitis complicated by melomonocyte proliferation. It exhibits proteolytic activity towards a range of substrates. It is physiologically inhibited by α1-antitrypsin. The protein has been described as having antibiotic and growth-promoting properties and causing emphysema when administered by tracheal insufflation. Proteinase 3 (PR-3) is also known as myeloblastin and p29b.
Physical form
Frozen in 50 mM MES, pH 4.5 with 700 mM NaCl.Параметрыbiological source human assay 95% (SDS-PAGE) form frozen liquid mol wt 29 kDa packaging pkg of 25 µg UniProt accession no. P24158, shipped in dry ice storage temp. 70°C Gene Information human ... AGP7(5657)
Safety InformationRIDADR NONH for all modes of transport WGK Germany nwg Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Proteinase from Aspergillus melleus
CAS Number: 9001-92-7 EC Number: 232-642-4 MDL number: MFCD00132092 eCl@ss: 32160410 NACRES: NA.54
Кат. номер P4032-5G P4032-25G P4032-100G ApplicationProteinase is an enzyme used to break down proteins by hydrolyzing peptide bonds. Proteinase is used to degrade proteins, to study proteinase inhibitors and to study thermal inactivation kinetics. Proteinase is used in nucleic acid isolation procedures in incubations. It is used to study proteinase-activated receptors, such as the transducers of proteinase-mediated signaling in inflammation and the immune response. Product P4032 is from Aspergillus melleus and has been used to non-specifically degraded xylanase from Streptomyces halstedii.
Packaging
5, 25 g in glass bottle
Biochem/physiol Actions
Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate .
Unit Definition
One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent), unless otherwise indicated.Параметрыtype Type XXIII Quality Level 200, form solid specific activity 3 units/mg solid storage temp. 2-8°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment dust mask type N95 (US),, Eyeshields,, Faceshields,, Gloves, RIDADR NONH for all modes of transport WGK Germany WGK 1 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Proteinase, bacterial
CAS Number: 9014-01-1 Enzyme Commission (EC) Number: 3.4.21.62 ( BRENDA | IUBMB ) EC Number: 232-752-2 MDL number: MFCD00132092 eCl@ss: 32160410 NACRES: NA.54
Кат. номер P8038-1G P8038-50MG P8038-250MG P8038-100MG
Specificity
Subtilisin A is a member of the Serine S8 Endoproteinase family. It has broad specificity with a preference for a large uncharged residue in the P1 position. It hydrolyzes native and denatured proteins, and is active under alkaline conditions.ApplicationThis is a proteolytic enzyme isolated from the fermentation of Bacillus licheniformis. It is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. Product P8038, also known as Subtilisin Carlsberg, has been used to hydrolyze cardiac cells to study the silencing of cardiac mitochondrial NHE1.
The enzyme from Sigma has been used to optimize release of all mitochondrial populations from homogenized ventricular tissue of rat heart. It has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax-embedded liver specimens for detecting human and viral DNA.
Packaging
1 g in glass bottle
50, 100, 250 mg in glass bottle
Biochem/physiol Actions
Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate .
Physical properties
Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa.
Unit Definition
One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).
Analysis Note
Amino acid analysis and isoelectric focusing electrophoresis consistent with subtilisin Carlsberg.ПараметрыQuality Level 200, type Type XXIV form lyophilized powder specific activity 0.05 Kunitz units/mg solid RNase, 5.0 Kunitz units/mg solid DNase, 7.0-14.0 units/mg solid mol wt 27 kDa purified by crystallization shipped in wet ice storage temp. 20°C
Safety Informationpictograms GHS05,GHS07,GHS08,GHS09 signalword Danger hcodes H302 - H315 - H318 - H334 - H335 - H410 pcodes P273 - P280 - P301 + P312 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment dust mask type N95 (US),, Eyeshields,, Faceshields,, Gloves, RIDADR UN 3082 9 / PGIII WGK Germany WGK 1 Узнать цену -
Pyroglutamate Aminopeptidase from Pyrococcus furiosus
Enzyme Commission (EC) Number: 3.4.19.3 ( BRENDA | IUBMB ) EC Number: 232-981-8 MDL number: MFCD00132139 NACRES: NA.54
Кат. номер P6236-.01UN-PW P6236-.01UN General descriptionPyroglutamate Aminopeptidase from Pyrococcus furiosus, also called the deblocking aminopeptidase, is a 42 kDa protein and belongs to aminopeptidase A family. It shares sequence homology with aminopeptidase in the active site, with conserved zinc and cobalt binding residues.ApplicationThe enzyme from Sigma has been used for the removal of pyroglutamate (pGlu) N-terminal blocking group, under reduced conditions, prior to N-terminal sequencing of purified cassiicolin.
Pyroglutamate Aminopeptidase, from Pyrococcus furiosus is a recombinant, thermostable aminopeptidase that is expressed in Escherichia coli. It is used to cleave pyroglutamic acid which allows analysis of N-terminal sequences of peptides.
Thermostable aminopeptidase that liberates N-terminal pyroglutamic acid from proteins and peptides prior to Edman degradation.
Biochem/physiol Actions
This enzyme is specific for N-terminal pyroglutamic acids. It cleaves the N-terminal pyroglutamic acid from proteins and peptides prior to Edman degradation. The optimal temperature range is 95 to 100 °C and the optimal pH range is 6.0 to 9.0.
Pyroglutamate Aminopeptidase (PGP 1) interacts with immunoglobulin, functions as inflammatory cytokine and modulates immune response. The levels PGP 1 is elevated during inflammation.
Unit Definition
One unit will hydrolyze 1 μmol of pyroglutamate p-nitroanilide per minute at pH 7.0 at 37 °C.
Physical form
Lyophilized powder containing sodium phosphate
Preparation Note
Reconstitute the vial of enzyme with 50 μl of 50 mM sodium phosphate, pH 7.0, with 10 mM DTT and 1 mM EDTA. The reconstituted solution should be stored at -20 °C.ПараметрыQuality Level 200, recombinant expressed in E. coli assay ~90% (SDS-PAGE) form lyophilized powder specific activity 5.0 units/mg protein mol wt 24.072 kDa by amino acid sequence, 28 kDa by SDS-PAGE shipped in dry ice storage temp. 20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment Eyeshields,, Gloves,, type N95 (US), RIDADR NONH for all modes of transport WGK Germany WGK 3 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Pyroglutamate Aminopeptidase from Pyrococcus furiosus, recombinant from E. coli
CAS Number: 9075-21-2 Enzyme Commission (EC) Number: 3.4.19.3 ( BRENDA | IUBMB ) EC Number: 232-981-8 MDL number: MFCD00132139
PackagingКат. номер 19924-1PAK-F 19924-.01UN-F 19924-10000UN-F
package of 0.01 Unit
Unit Definition
1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol Pyroglutamate-p-nitroanilide per minute at pH 7.0 and 37 °C
Analysis Note
enzyme activity: the optimum temperature is 95-100 °C (the enzyme is stable up to 75 °C), the optimum pH is 6-9 (stable from pH 6-9). Inhibitors: PCMB, Hg+.Other NotesAn enzyme that removes pyroglutamic acid (pGlu) from pGlu-peptide and proteins; employed in Edman degradation.ПараметрыQuality Level 100, form lyophilized specific activity 7-13 mU (per vial) mol wt Mr ~28000 storage temp. 20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P261 - P305 + P351 + P338 - P342 + P311 Target Organs Respiratory system RIDADR NONH for all modes of transport WGK Germany WGK 3 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Rennin from calf stomach
CAS Number: 9001-98-3 Enzyme Commission (EC) Number: 3.4.23.4 ( BRENDA | IUBMB ) EC Number: 232-645-0 MDL number: MFCD00132173 NACRES: NA.54
Кат. номер R4877-100MG R4877-2MG R4877-5MG R4877-25MG ApplicationRennin, also known as chymosin, is a milkclotting acid proteinase produced in the stomach of a calf. It is used in cheesemaking and to study neonatal gastric digestion .
Packaging
100 mg in glass bottle
Package size based on protein content
Biochem/physiol Actions
Rennin, a 323 amino acid chain, is secreted as an inactive precursor which is then converted into an active enzyme through limited proteolysis. It cleaves the peptide bond between phenylalanine and methionine in K-Casein.
Unit Definition
One unit will coagulate 10 mL of milk per min at 30 °C.
Physical form
Lyophilized powder containing sodium chloride
Analysis Note
Protein determined by biuret.Параметрыform lyophilized powder Quality Level 200, specific activity ≥20 units/mg protein purified by crystallization composition Protein, ≥40% storage temp. −20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system RIDADR NONH for all modes of transport WGK Germany WGK 3 Узнать цену -
Rennin from Mucor miehei
CAS Number: 9073-79-4 Enzyme Commission (EC) Number: 3.4.23.23 ( BRENDA | IUBMB ) EC Number: 232-975-5 MDL number: MFCD00132171 NACRES: NA.54
Unit DefinitionКат. номер 83553-1G 83553-5G
1 U corresponds to the amount of enzyme which liberates 1 μmol folin-positive amino acids and peptides (calculated as tyrosine) per minute at pH 7.5 and 37°C (casein, Cat. No. 22078, as substrate)Other NotesAction on a synthetic chromophoric hexapeptide
Sales restrictions may applyПараметрыform powder quality lyophilized specific activity ~0.1 U/mg mol wt Mr ~40000 color slightly brown storage temp. 20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment dust mask type N95 (US),, Eyeshields,, Faceshields,, Gloves, RIDADR NONH for all modes of transport WGK Germany WGK 1 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
SUMO Protease
Кат. номер SAE0067-2500UN SAE0067-2500UN-PW General descriptionSUMO proteases are a general class of enzymes that specifically remove the post-translational protein modification (PTM) known as small ubiquitin-related modifier (SUMO), which falls into the PTM class of ubiquitin and/or ubiquitin-like proteins (UBL). The enzyme commonly referred to as ‘SUMO protease is the Ubl-specific protease 1 (Ulp1) from Saccharomyces cerevisiae. This was the first of this class of enzymes to be isolated. SUMO protease specifically cleaves the SUMO moiety in a ‘scarless manner. SUMO protease recognizes the tertiary structure of the Ubiquitin-like SUMO domain and hydrolyzes the peptide bond in the x–Gly–Gly–x sequence after the Gly-Gly bond, at the C-terminus of the SUMO domain. In addition to cleavage of natural SUMO-modified proteins, SUMO protease is used to cleave recombinant SUMO fusion proteins. The SUMO domain is a known solubility-enhancing fusion tag used in recombinant protein expression. A histidine tag can also be added at the N-terminus of the SUMO domain as a purification tag. This SUMO protease product carries a 6x histidine tag. Thus it can be easily removed together with the cleaved SUMO domain, following the digestion reaction
SUMO protease is active over a wide range of temperatures (2–30 °C), ionic strengths (0–400 mM NaCl), and pH ranges (6–8.5). However, its activity may vary depending on the substrate and conditions. Researchers will need to optimize their specific reaction conditions. As an initial suggestion, 20 units of SUMO protease can be used per mg of target protein for 1 hour at 30 °C, or overnight at 2–8 °C. The cleavage efficiency can then be estimated by SDS-PAGE. If necessary, the amount of SUMO protease can then be adjusted. SUMO protease works better in the presence of reducing agents, e.g., 0.5–2 mM DTT. DTT in the reaction mixture can significantly enhance cleavage efficiency, especially during longer incubations
Store the reconstituted product at –20 °C. It is recommended to reconstitute the enzyme in 100 µL of either water or 50% glycerol (v/v), supplemented with 1 mM DTT. Solutions in water/DTT should be stored in frozen aliquots to avoid freeze-thaw cycles, which can adversely affect the protease activity.Unit DefinitionOne enzyme unit is defined as the amount that will cut 90% of 100 pmol of SUMO-GST in 1 hour at 30°C.ПараметрыQuality Level 200 recombinant expressed in E. coli assay 95% (SDS-PAGE) form lyophilized powder mol wt 27 kDa shipped in ambient storage temp. 20°C
Safety InformationRIDADR NONH for all modes of transport WGK Germany WGK 2 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
SUMO Protease, Biotin tagged SAE0101-2500UN
General descriptionSUMO proteases are enzymes that specifically cleave the post-translational protein modification (PTM) known as small ubiquitin-related modifier (SUMO). SUMO falls into the PTM class of ubiquitin and/or ubiquitin-like proteins (UBL).SUMO protease is the Ubl-specific protease 1 (Ulp1) from Saccharomyces cerevisiae. This was the first of this class of enzymes to be isolated. SUMO protease cleaves specifically the SUMO moiety in a ‘scarless manner. After recognizing the tertiary structure of the Ubiquitin-like SUMO domain, SUMO protease hydrolyzes the peptide bond in the x–Gly–Gly–x sequence after the Gly-Gly bond, at the C-terminus of the SUMO domain. Besides the cleavage of natural SUMO-modified proteins, SUMO protease is used to cleave recombinant SUMO fusion proteins. The SUMO domain is a known solubility-enhancing fusion tag used in recombinant protein expression. Since this recombinant protease does not contain any coman protein purification tag it can be used for on-column cleavage of column bound SUMO fusion protein. Sumo protease with Biotin tag can be easily removed at the end of the digestion reaction.ApplicationThis biotin-tagged SUMO protease product is designed to be used for on-column cleavage of SUMO fusion proteins. This method specifically cleaves the protein of interest from a column-bound SUMO fusion protein, leaving the SUMO domain bound to the affinity column (e.g. Ni-NTA column) and eluting only the protein of interest. This method is advantageous to post-elution cleavage for several reasons:
Eliminates most of the impurities normally associated with purification on Ni-chelating columns.- Allows much gentler elution conditions, with an added flexibility in the composition of the elution buffer.
- Assist preventing protein aggregation and inactivation.
- Following cleavage, the protease can be efficiently removed by using any avidin-conjugated or streptavidin-conjugated beads.
This biotin-tagged SUMO protease has been enzymatically biotinylated without affecting its proteolytic activity. It does not include any additional protein purification tag (e.g., histidine-tag or GST).
Unit Definition
One enzyme unit is defined as the amount that will cut 90% of 100 pmol of SUMO-GST in 1 hour at 30°C.Параметрыassay ≥90% (SDS-PAGE) form aqueous solution mol wt 27 kDa concentration ≥25,000 units/mL shipped in dry ice storage temp. −20°C
Safety InformationWGK Germany WGK 2 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Thermolysin from Geobacillus stearothermophilus
CAS Number: 9073-78-3 Enzyme Commission (EC) Number: 3.4.24.27 ( BRENDA | IUBMB ) EC Number: 232-973-4 MDL number: MFCD00165549 eCl@ss: 32160410
Кат. номер P1512-1G P1512-100MG P1512-250MG P1512-25MG P1512-10MG General descriptionThermolysin is a protease that has specificity different from other proteases available for sequence investigations.ApplicationThermolysin has been shown to have a prosequeence that acts as an intramolecular chaperone in vivo. It has also been used in a study to investigate the effects of sodium chloride on thermal stability and catalytic activity.
Thermolysin is also commonly used for the commercial synthesis of N-(benzyloxycarbonyl)-L-aspartyl-L-phenylalanine methyl ester, the precursor for the artificial sweetener aspartame.
Non-specific Protease Activity Assay Video
A thermostable (thermophilic) extracellular metalloendopeptidase containing four calcium ions. Cofactors are zinc and calcium. Hydrolyzes protein bonds on the N-terminal side of hydrophobic amino acid residues. The pH optimum is 8.0 and the optimal temperature for activity is 70 °C. Considerably stable from pH 5 to 9.5. Thermolysin has a low cleavage specificity, therefore, it produces a number of short fragments that are suitable for sequencing. Preferential cleavage: X-cleavage-Y-Z where X=any amino acid; Y=Leu, Phe, Ile, Val, Met, Ala and Z is any amino acid other than Pro. Cleavage N-terminal to Leu is preferred over cleavage of N-terminal to Phe which is preferred over the others. Often used to do limited proteolysis for peptide mapping and studies of protein structure and conformational changes.
Packaging
25 mg in poly bottle
1 g in glass bottle
100, 250 mg in glass bottle
Quality
Contains many extraneous enzymes.
Unit Definition
One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).
Physical form
lyophilized powder containing calcium and sodium acetate buffer salts
Preparation Note
The pH optimum is 8.0 and the optimal temperature for activity is 70 °C. Considerably stable from pH 5 to 9.5. Thermolysin has a low cleavage specificity, therefore, it produces a number of short fragments that are suitable for sequencing. Preferential cleavage: X-cleavage-Y-Z where X=any amino acid; Y=Leu, Phe, Ile, Val, Met, Ala and Z is any amino acid other than Pro. Cleavage N-terminal to Leu is preferred over cleavage of N-terminal to Phe which is preferred over the others.Параметрыtype Type X Quality Level 200, form lyophilized powder specific activity 30-350 units/mg protein (E1%/280) mol wt 34.6 kDa by amino acid sequence purified by crystallization shipped in wet ice storage temp. 20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H317 - H319 - H334 - H335 pcodes P261 - P280 - P305 + P351 + P338 - P342 + P311 Target Organs Respiratory system Personal Protective Equipment dust mask type N95 (US),, Eyeshields,, Faceshields,, Gloves, RIDADR NONH for all modes of transport WGK Germany WGK 3 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Thimet Oligopeptidase from Bacillus licheniformis
Enzyme Commission (EC) Number: 3.4.24.15 ( BRENDA | IUBMB ) NACRES: NA.54
Кат. номер T7705-100UN T7705-100UN-PW General descriptionThimet oligopeptidase is considered essential in the degradation of collagen in collaboration with collagenolytic enzymes. Thimet oligopeptidase (TOP) is a neuropeptidase involved in the hydrolysis of gonadotropin-releasing hormone, a key component of the hypothalamic-pituitary-gonadal axis.ApplicationThimet oligopeptidase can be used for the degradation of collagen in combination with collagenases. It can also be used for the hydrolysis of neuropeptides such as bradykin, neurotensin, and amyliod-β-peptide. Thimet oligopeptidase has been used in a study to investigate the effect of acute cocaine administration in male rats on TOP specific activity and mRNA levels in prosencephalic brain areas related with the reward circuitry: ventral striatum, hippocampus, and frontal cortex.
Preparation Note
This enzyme has been affinity chromatographically purified using a niquel affinity column. It contains a 6-Histidine tag in its C-terminus.
A working solution of this enzyme can be prepared in 20 mM phosphate buffered saline solution, pH 7.0, or sterile and deionized water, pH 7.0.ПараметрыQuality Level 200, recombinant expressed in E. coli form powder mol wt ~77 kDa storage temp. 20°C
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Trypsin Acetylated from bovine pancreas
Enzyme Commission (EC) Number: 3.4.21.4 ( BRENDA | IUBMB ) MDL number: MFCD00082094 NACRES: NA.54
Кат. номер T6763-1G T6763-100MG T6763-250MG T6763-5G T6763-25MG General descriptionThe trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.ApplicationTrypsin has been used in a study to assess the ontogeny of the endocrine pancreas in the fetal/newborn baboon. Trypsin digestion and hydrogen/deuterium exchange support the transition between inward- and outward-facing conformations during the catalytic cycle of the bacterial multidrug ATP-binding cassette transporter.
Packaging
1 g in glass bottle
100, 250 mg in glass bottle
Biochem/physiol Actions
Lys-acetylated trypsin is less susceptible to autolysis than the native form.
Unit Definition
One BAEE unit will produce a A253 of 0.001 per min at pH 7.6 at 25° C using BAEE as substrate. Reaction volume = 3.2 mL (1 cm light path).
Preparation Note
Prepared by the method of Labouesse, J. and Gervais, M., Eur. J. Biochem., 2, 215 (1967).ПараметрыQuality Level 200 type Type V-S form powder specific activity 8,500 BAEE units/mg protein (biuret) UniProt accession no. Q29463, storage temp. 20°C Gene Information cow ... TRYP8(282603)
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment dust mask type N95 (US),, Eyeshields,, Faceshields,, Gloves, RIDADR NONH for all modes of transport WGK Germany WGK 3 Узнать цену -
Trypsin Agarose
Enzyme Commission (EC) Number: 3.4.21.4 ( BRENDA | IUBMB ) MDL number: MFCD00082094 eCl@ss: 42020142 NACRES: NA.54
Кат. номер T1763-25UN T1763-10UN T1763-50UN General descriptionTrypsin Agarose is an insoluble enzyme product. It is produced by reacting a conventional "soluble" enzyme (trypsin) with an inert base (agarose). This insoluble conjugate retains the activity of the original enzyme. Trypsin bound to agarose are highly stable and maintain denaturing conditions for longer time than the soluble trypsin.
The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.ApplicationA very active and very stable trypsin agarose derivative has been used to optimize the design of the synthesis of a model dipeptide, benzoylarginine leucinamide. Trypsin has also been used in a study to investigate protonation-state determination in proteins using high-resolution X-ray crystallography.
Trypsin Agarose has been used for enzymatic hydrolysis of prolamins and gliadin to generate peptides.
Packaging
50 units in glass bottleOther NotesInsolubilized
Unit Definition
One unit will hydrolyze 1.0 μmole of BAEE per min at pH 8.0 at 30 °C (titrimetric assay).
Physical form
Suspension in approx. 10 mM acetic acid, pH 3.2Параметрыbiological source bovine pancreas (trypsin) Quality Level 200, form buffered aqueous suspension concentration ≥15 units/mL (packed gel) extent of labeling ≥15 units per mL packed gel matrix cross-linked beaded agarose shipped in wet ice storage temp. 2-8°C
Safety Informationpictograms GHS07 signalword Warning hcodes H315 - H317 - H319 - H335 pcodes P280 - P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment Eyeshields,, Faceshields,, Gloves,, type ABEK (EN14387) respirator filter, RIDADR NONH for all modes of transport WGK Germany WGK 3 Узнать цену -
Trypsin from bovine pancreas
CAS Number: 9002-07-7 Enzyme Commission (EC) Number: 3.4.21.4 ( BRENDA | IUBMB ) EC Number: 232-650-8 MDL number: MFCD00082094 NACRES: NA.54
Кат. номер T1426-1G T1426-PM T1426-100G T1426-100MG T1426-5G T1426-250MG T1426-500MG T1426-50MG T1426-100UG ApplicationFor trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. The typical use for this product is in removing adherent cells from a culture surface. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. Trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestions. Additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps.Packaging50, 100, 250, 500 mg in glass bottle
1, 5, 100 g in glass bottleBiochem/physiol ActionsTrypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity.
Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin.ComponentsTrypsin consists of a single chain polypeptide of 223 amino acid residues, produced by the removal of the N-terminal hexapeptide from trypsinogen which is cleaved at the Lys - lle peptide bond. The sequence of amino acids is cross-linked by 6 disulfide bridges. This is the native form of trypsin, beta-trypsin. BETA-trypsin can be autolyzed, cleaving at the Lys - Ser residue, to produce alpha-trypsin. Trypsin is a member of the serine protease family.CautionSolutions in 1 mM HCl are stable for 1 year in aliquots and stored at -20°C. The presence of Ca2+ will also diminish the self-autolysis of trypsin and maintain its stability in solution. Trypsin will also retain most of its activity in 2.0 M urea, 2.0 M guanidine HCl, or 0.1% (w/v) SDS.Unit DefinitionOne BAEE unit will produce a A253 of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate.Preparation NoteSoluble in 1 mM HCl at 1 mg/mL.
It is also TPCK-treated and dialyzed. Treatment with L-1-Tosylamide-2-phenylethyl chloromethyl ketone (TPCK) reduces the chymotrypsin activity which is usually present in trypsin.ПараметрыQuality Level 200 form essentially salt-free, lyophilized powder specific activity ≥10,000 BAEE units/mg protein mol wt 23.8 kDa solubility hydrochloric acid: soluble 1 mM Featured Industry Diagnostic Assay Manufacturing foreign activity Chymotrypsin ≤0.1 BTEE units/mg protein storage temp. −20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P261 - P264 - P271 - P280 - P302 + P352 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment dust mask type N95 (US), Eyeshields, Faceshields, Gloves RIDADR NONH for all modes of transport WGK Germany WGK 1 Узнать цену -
Trypsin from human pancreas
CAS Number: 9002-07-7 Enzyme Commission (EC) Number: 3.4.21.4 ( BRENDA | IUBMB ) EC Number: 232-650-8 MDL number: MFCD01323069 NACRES: NA.54
Кат. номер T6424-1VL-PW T6424-1VL General descriptionThe trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.
Trypsin is a serine protease. The pancreas produce the precursor trypsinogen and secretes it to the intestine. Trypsinogen is converted to trypsin by enterokinase in the intestinal mucous membrane.ApplicationTrypsin has been used in a study to assess the similarities between the hepatitis E virus and human astrovirus. Trypsin has also been used in a study to characterize a unique technique for culturing primary adult human epithelial progenitor, or stem, cells.
Unit Definition
One BAEE unit will produce a A253 of 0.001 per min at pH 7.6 at 25 °C using BAEE as substrate. Reaction volume = 3.2 mL (1 cm light path).
Quantity
Minimum 1,000 BAEE units/vial
Analysis Note
Protein determined by E1%/280.ПараметрыQuality Level 200 form salt-free, lyophilized powder packaging vial of 1,000 BAEE units UniProt accession no. P07477,","P07478,","P35030, storage temp. 20°C Gene Information human ... PRSS1(5644), PRSS2(5645), PRSS3(5646)
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Trypsin from porcine pancreas
CAS Number: 9002-07-7 Enzyme Commission (EC) Number: 3.4.21.4 ( BRENDA | IUBMB ) EC Number: 232-650-8 MDL number: MFCD00082094
Кат. номер T0303-10G T0303-PM T0303-1G T0303-100G ApplicationFor trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. The typical use for this product is in removing adherent cells from a culture surface. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. Trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestionsns†. Additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps.
Packaging
1, 10 g in poly bottle
Biochem/physiol Actions
Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity.
Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin.
Components
Trypsin consists of a single chain polypeptide of 223 amino acid residues, produced by the removal of the N-terminal hexapeptide from trypsinogen which is cleaved at the Lys - lle peptide bond. The sequence of amino acids is cross-linked by 6 disulfide bridges. This is the native form of trypsin, beta-trypsin. BETA-trypsin can be autolyzed, cleaving at the Lys - Ser residue, to produce alpha-trypsin. Trypsin is a member of the serine protease family.
Caution
Solutions in 1 mM HCl are stable for 1 year in aliquots and stored at -20°C. The presence of Ca2+ will also diminish the self-autolysis of trypsin and maintain its stability in solution. Trypsin will also retain most of its activity in 2.0 M urea, 2.0 M guanidine HCl, or 0.1% (w/v) SDS.
Unit Definition
One BAEE unit will produce a A253 of 0.001 per min at pH 7.6 at 25° C using BAEE as substrate. One BTEE unit = 320 ATEE units. Reaction volume = 3.2 mL (1 cm light path).
Preparation Note
This product is a lyophilized powder soluble in Hank′s Balanced Salt Solution at 25 mg/mL.ПараметрыQuality Level 200, type Type IX-S form lyophilized powder specific activity 13,000-20,000 BAEE units/mg protein mol wt 23.8 kDa Featured Industry Diagnostic Assay Manufacturing foreign activity chymotrypsin ≤1.0 units/mg protein storage temp. −20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P261 - P264 - P271 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment dust mask type N95 (US),, Eyeshields,, Faceshields,, Gloves, RIDADR NONH for all modes of transport WGK Germany WGK 1 Узнать цену -
Trypsin inhibitor from Glycine max (soybean)
CAS Number: 9035-81-8 EC Number: 232-906-9 MDL number: MFCD00082103 NACRES: NA.54
Кат. номер T9003-CP T9003-100MG T9003-100MG-KC 2550055 T9003-5G T9003-1G T9003-250MG T9003-25MG T9003-500MG T9003-500G T9003-100G ApplicationTrypsin has been used in a study to assess the potential application in animal cell culture of an alkaline protease from a non-toxigenic mangrove isolate of Vibrio sp. V26. Trypsin has also been used in a study to improve the detection of fungi in eosinophilic mucin.
Packaging
25 mg in poly bottle
1, 5 g in glass bottle
100, 250, 500 mg in glass bottle
Biochem/physiol Actions
This inhibitor acts against trypsin, and chymotrypsin and plasmin to a lesser extent. It will also inhibit proteases with mechanisms similar to trypsin, plasma kallikrein and coagulation Factor X. The trypsin inhibitor will not act against metalloproteases, tissue-baseed kallikrein, acid proteases, or thio proteases. This inhibitor acts by forming a 1:1 stoichiometric complex with the protease active site, and then cleaving a single arginine-isoleucine bond on the inhibitor. The inhibition is both reversible and pH dependent.
Components
The soybean trypsin inhibitor is a monomeric protein containing 181 amino acid residues in a single polypeptide chain crosslinked by two disulfide bridges.
Unit Definition
One trypsin unit will produce a A253 of 0.001 per min with BAEE as substrate at pH 7.6 at 25 °C; reaction volume 3.2 ml, 1 cm light path.
One trypsin unit = A253 of 0.001 per minute with N-alpha-benzoyl-L-arginine ethyl ester (BAEE) as substrate at pH 7.6 at 25 °C.
Preparation Note
The trypsin inhibitor is soluble in water and phosphate buffers at 10 mg/mL. It is soluble in balanced salt solutions at 1 mg/mL and in serum-free media. Concentrated solutions greater than 10 mg/mL may be hazy and have a yellow to amber color. After trypsinizing cells, resuspend in 1 mL trypsin inhibitor solution at 1 mg/mL for every mL of trypsin solution used for dissociation. The cell suspension should then be centrifuged at 1000 rpm, forming a cell pellet.
Solutions can retain activity when stored short-term at 2-8° C. Solutions are stable in frozen aliquots at -20°C.
Analysis Note
One mg of trypsin inhibitor will inhibit 1.0-3.0 mg trypsin of activity ~10,000 BAEE units per mg protein.Параметрыbiological source Glycine max (soybean) Quality Level 300, form lyophilized powder mol wt 20.1 kDa solubility H2O: >10 mg/mL, phosphate buffer: >10 mg/mL (hazy above 10 mg/ml), soluble Featured Industry Diagnostic Assay Manufacturing storage temp. 2-8°C
Safety Informationpictograms GHS08 signalword Danger hcodes H317 - H334 pcodes P261 - P272 - P280 - P284 - P302 + P352 - P333 + P313 Personal Protective Equipment Eyeshields,, Gloves,, type N95 (US), RIDADR NONH for all modes of transport WGK Germany WGK 3 Узнать цену -
Trypsin Pancreas from human pancreas SRP6311-50UG
NACRES: NA.32 General descriptionTrypsin hydrolyzes peptides, amides, and ester bonds involving the carboxyl groups of L-arginine or L-lysine. Increased serum values of this enzyme and/or its zymogen (trypsinogen) have been found in patients with cystic fibrosis. Trypsinogen has three isoforms: cationic (trypsinogen 1), anionic (trypsinogen 2, MW - 22.5 kDa), and mesotrypsinogen (trypsinogen 3, MW - 25 kDa). The trypsin available is the cationic form.
Physical form
Lyophilized from 2 mM HCl.
Reconstitution
In water or aqueous bufferПараметрыbiological source human assay 95% (SDS-PAGE) form lyophilized mol wt 21-23 kDa packaging pkg of 50 µg UniProt accession no. P07477, shipped in wet ice storage temp. 20°C Gene Information human ... TRYP1(5644)
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P261 - P264 - P271 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 Target Organs Respiratory system RIDADR NONH for all modes of transport WGK Germany WGK 1 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Trypsin Sequencing Grade, modified
Enzyme Commission (EC) Number: 3.4.21.4 ( BRENDA | IUBMB )
Кат. номер 11418033001 11418025001 General descriptionTrypsin Sequencing Grade, modified, is isolated from bovine pancreas as a highly purified and specific protease, and subsequently modified.
Inhibitors: TLCK, DFP, PMSF, leupeptin, soybean trypsin inhibitor, trypsin inhibitor from hen egg, aprotinin, 2-macroglobulin,1-antitrypsin, APMSF, and antipain.SpecificityTrypsin is a serine endopeptidase. At pH 7.5–9, it specifically hydrolyzes proteins and peptide bonds C-terminally of Iysine and arginine. Amide and ester bonds of Arg and Lys are also cleaved. The specificity of Trypsin Sequencing Grade, modified, is verified with the oxidized B-chain of insulin (insulin Box) as a substrate. High concentrations of Trypsin Sequencing Grade, modified, one part by weight enzyme with 9 parts by weight insulin Box, are incubated for 18 hours to detect traces ofchymotrypsin impurities.ApplicationUse Trypsin Sequencing Grade, modified, to generate glycopeptides from purified glycoproteins.
It is used for:- Protein-structure elucidation
- Tryptic mapping
- Fingerprinting analysis
- Sequence analysis
- Translocation studies
- Protein identification
QualityPurity: Free of impurities that may interfere with the separation of peptides in reversed-phase HPLC.Preparation NoteWorking concentration: 1/100 to 1/5 of the protein by weight
Storage conditions (working solution): -15 to -25 °C
Trypsin Sequencing Grade, modified, is more resistant to autolysis, even at pH values in the neutral and weakly basic range. The enzyme can be used in high concentrations.
A solution in 1% acetic acid or 1 mM HCI can be used for up to one week when stored at 2 to 8° C. Stored in aliquots at -15 to -25 °C, the solution is stable for at least one year without loss of activity.Other NotesFor life science research only. Not for use in diagnostic procedures.ПараметрыQuality Level 100 form lyophilized (salt-free) packaging pkg of 4 x 100 μg (11418033001), pkg of 4 x 25 μg (11418025001) Торговая марка Roche optimum pH 8.0 shipped in wet ice storage temp. 2-8°C
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Trypsin, Bovine Pancreas
CAS Number: 9002-07-7 Enzyme Commission (EC) Number: 3.4.21.4 ( BRENDA | IUBMB )
Кат. номер 6502-50GM 6502-300GM 6502-2.5MU 6502-200GM 6502-25MU 6502-25GM 6502-2.5MUCN 6502-25MUCN General descriptionNative trypsin from bovine pancreas. Serine protease that specifically hydrolyzes amides, peptides, and proteins at the C-terminus side of arginine and lysine residues. Inhibitors include aprotinin, DFP, and soybean trypsin inhibitor. Has an optimal pH of 8.5-8.8.
Note: 1 NF unit = 1 USP unit = 3 SU at 30°C, pH 7.6; 1 TAME unit = 19.2 USP units = 57.5 BAEE units; 1 MU = 1,000,000 units.
Native trypsin from bovine pancreas. Serine protease that specifically hydrolyzes amides, peptides and proteins at the C-terminal side of arginine and lysine residues. Inhibitors include aprotinin, DFP, and soybean trypsin inhibitor. Note: 1 MU = 1,000,000 units.
Packaging
25 mu in Plastic ampoule
2.5 mu in Glass bottle
Warning
Toxicity: Irritant (B)
Unit Definition
One USP unit is defined as the amount of enzyme that will digest BAEE and cause an increase in absorbance of 0.003 units at 253 nm per min at 25°C, pH 7.6.
Physical form
Salt-free
Reconstitution
Following reconstitution in HCl, aliquot and freeze (-20°C) for long-term storage or refrigerate (4°C) for short-term storage. Dilute into aqueous buffers (at neutral pH) just prior to use. Following reconstitution in H₂O or buffer, use immediately or aliquot and freeze (-70°C) to minimize autolysis. HCl stock solutions are stable for up to 1 week at 4°C or for up to 1 month at -20°C. H₂O or buffer stock solutions are stable for up to 1 month at -70°C.Other NotesBergmeyer, H.U. 1983. Methods of Enzymatic Analysis, 3rd ed. Vol. 3, 17.
Kostka, V., and Carpenter, F.H. 1964. J. Biol. Chem.239, 1799.
Hummel, B.C.W. 1955. Can. J. Biochem. Physiol.37, 1393.Legal InformationCALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, GermanyПараметрыstorage conditions -20C Quality Level 100, form solid specific activity 2,500 USP units/mg dry wt Торговая марка Calbiochem® storage condition OK to freeze, desiccated (hygroscopic) solubility HCl: 1 mM, neutral buffer: soluble, water: soluble foreign activity Chymotrypsin 50 NF units/mg dry wt. shipped in ambient storage temp. 20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P261 - P264 - P271 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 Target Organs Respiratory system WGK Germany WGK 1 Узнать цену -
Trypsin, Iodination Grade, Human Pancreas
CAS Number: 9002-07-7 Enzyme Commission (EC) Number: 3.4.21.4 ( BRENDA | IUBMB )
Кат. номер 650275-100UG 650275-200UG 650275-50UG 650275-1MG 650275-50UGCN General descriptionNative trypsin from human pancreas. Serine protease that specifically hydrolyzes amides, peptides, and proteins at the C-terminus side of arginine and lysine residues.
Packaging
50 μg in Plastic ampoule
Warning
Toxicity: Irritant (B)
Unit Definition
One unit is defined as the amount of enzyme that will hydrolyze 1 µmol of N-benzyl-L-arginine-pNA per min at 25°C, 200 mM Tris-HCl, pH 7.8, 20 mM CaCl.
Physical form
Salt-free.
Preparation Note
Prepared from tissue that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
Reconstitution
Following reconstitution, aliquot and freeze (-70°C).Other NotesMerck Index13, 9865.
Travis, J., and Roberts, R.C. 1969. Biochemistry 8, 2884.Legal InformationCALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, GermanyПараметрыstorage conditions -20C Quality Level 200 assay 95% (SDS-PAGE) form lyophilized solid specific activity 2.5 units/mg protein Торговая марка Calbiochem® storage condition OK to freeze","desiccated solubility HCl: 2 mM","aqueous buffer, pH 2.5: soluble foreign activity Chymotrypsin, none detected (when assayed against N-Suc-Ala-Ala-Pro-Phe-pNA (573462)) shipped in wet ice storage temp. 20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P261 - P264 - P271 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 Target Organs Respiratory system WGK Germany WGK 1 Узнать цену -
Trypsin, Porcine, MS Grade
Кат. номер 650279-1SET 650279-1SETCN General descriptionA chemically modified trypsin that is resistant to autolysis and degradation. Trypsin specifically hydrolyzes amides, peptides and proteins at the C-terminus side of arginine and lysine residues. This mass spectrometry grade trypsin is methylated, TPCK treated, and affinity purified. It is specifically designed for digestion of proteins for sequencing and peptide fragment analysis by mass spectrometry. A trypsin to protein ratio of 1:100 to 1:20 is recommended for mass spectrometry protocols. Note: 1 SET = 5 X 20 µg of modified trypsin, and 1 ml of resuspension buffer.
A chemically modified trypsin that is resistant to autolysis and degradation. Trypsin specifically hydrolyzes amides, peptides and proteins at the C-terminus side of arginine and lysine residues. This mass spectrometry grade trypsin is methylated, TPCK treated, and affinity purified. It is specifically designed for digestion of proteins for sequencing and peptide fragment analysis by mass spectrometry.
Packaging
1 set in Glass bottle
Warning
Toxicity: Harmful (C)
Unit Definition
One BAEE unit is defined as the ammount of enzyme required to produce a ΔA253 of 0.001 per min in a reaction volume of 3.2 ml at pH 7.6 at 25°C.
One BTEE unit is defined as the amount of enzyme required to hydrolyze 1 µmol BTEE per min at 25°C, pH 7.8
Reconstitution
Following reconstitution, aliquot and freeze (-°C). Unused stock solutions are stable for up to 2 weeks at -70°C. Avoid freeze/thaw cycles of solution.Other NotesHenzel, W.J., et al. 1993. PNAS90, 5011.
Rice, R.H., et al. 1977. Biochim Biophys Acta492, 316..Legal InformationCALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, GermanyПараметрыstorage conditions -20C Quality Level 100, form lyophilized specific activity 10,000 U/mg Торговая марка Calbiochem® storage condition OK to freeze foreign activity Chymostrypsin <3 BTEE units/mg solid shipped in wet ice storage temp. 20°C
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P302 + P352 - P304 + P340 - P305 + P351 + P338 - P342 + P311 Узнать цену -
TrypsinAgarose
MDL number: MFCD00082094 eCl@ss: 42020142 NACRES: NA.54
Кат. номер T4019-100UN T4019-50UN T4019-25UN General descriptionThe trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.ApplicationAn experimental approach using SDS-PAGE, in-gel trypsin digestion and proteomic analysis identified five endosomal proteins. Trypsin cleavage of the high-risk HPV-16 E5 protein (16E5) generates a unique four-amino acid C-terminal peptide that serves as a marker for E5 expression in transfected cells and epithelial cell lines containing integrated and episomal HPV-16 DNA.
Unit Definition
One unit will hydrolyze 1.0 μmole of BAEE per min at pH 8.0 at 30 °C (titrimetric assay).
Physical form
Suspension in approx. 10 mM acetic acid, pH 3.2, containing preservative
Preparation Note
TPCK-treatedПараметрыbiological source bovine pancreas (trypsin) Quality Level 200, form buffered aqueous suspension concentration ≥15 units/mL (packed gel) extent of labeling ≥15 units per mL (packed gel) matrix beaded agarose storage temp. 2-8°C
Safety Informationpictograms GHS07 signalword Warning hcodes H317 pcodes P261 - P272 - P280 - P302 + P352 - P333 + P313 - P362 + P364 RIDADR NONH for all modes of transport WGK Germany WGK 3 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Tryptase from human lung
Enzyme Commission (EC) Number: 3.4.21.59 ( BRENDA | IUBMB ) MDL number: MFCD00272854 PubChem Substance ID: 329826858 NACRES: NA.54
Кат. номер T7063-5UG T7063-5UG-PW T7063-10UG T7063-10UG-PW T7063-1UG General descriptionTryptase is a glycoprotein released from mast cells during anaphylaxis, which performs a number of functions including catalyzing the activation of complement C3, converting prostromelysin to stromelysin (MMP-3), and cleaving fibrinogen resulting in a loss of clotting potential. Human tryptase is a major secretory protease of human lung mast cells.ApplicationTryptase has been used in a study that purified and characterized recombinant rat mast cell protease 7 expressed in Pichia pastoris. Tryptase has also been used in a study to investigate drug allergies in mast cell disease.
Biochem/physiol Actions
Tryptase is a member of the serine protease S1 family. It is the predominant neutral protease of the mast cell granules. Within the mast cell granule it exists as a heparin-stabilized active tetramer. Stabilization is a result of the high negative charge density of the glycosaminoglycan. This stabilization activity is observed with heparins with a MW greater than 6 kDa as well as other glycosaminoglycans such as dextran sulfate or chondroitin sulfates. Removal of heparin results in dissociation of the tetramer and inactivation of the enzyme. High concentrations of NaCl will result in the dissociation of heparin.
Tryptase is released from the mast cell as a result of the degranulation response during anaphylaxis. In addition, several tryptase genes and alleles (, , & ) have been identified in various tissues and circulating in blood. Pro--tryptase is thought to be the constituative circulating form in blood.
The biological function of tryptase is unknown. However it has been reported to catalyze the activation of complement C3, convert prostromelysin to stromelysin (MMP-3), and cleave fibrinogen resulting in a loss of clottting potential. Tryptase also degrades fibronectin, calcitonin gene-related peptide, vasoactive intestinal peptide,
and kininogen.
Quality
Highly purified
Physical properties
Molecular Weight: ~135 kDa (Human)(Non-covalently linked tetramer with two sets of dissimilar subunits possibly resulting from heterogeneity in N-linked glycosylation and existence of a & b isoforms sequences in human lung). 31-33 kDa (Monomer MW)
Unit Definition
One unit will hydrolyze 1.0 μmole of N-benzyl-DL-Arg-pNA per minute at pH 8 at 25 °C.
Physical form
Supplied as a liquid in 50mM Sodium Acetate, 1M Sodium Chloride, pH 5.0 with 0.05mM Heparin and 0.01% Sodium AzideПараметрыform buffered aqueous solution Quality Level 200 specific activity 5 units/mg protein mol wt ~135 kDa UniProt accession no. P20231,","Q15661,","Q9BZJ3,","Q9NRR2, shipped in dry ice storage temp. 20°C SMILES string CC(O)=O.Cc1cc(NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](Cc2ccccc2)NC(=O)OC(C)(C)C)cc3OC(=O)C=Cc13 InChI 1S/C33H43N7O8.C2H4O2/c1-19-15-21(17-26-22(19)12-13-27(42)47-26)37-28(43)23(11-8-14-36-31(34)35)38-30(45)25(18-41)39-29(44)24(16-20-9-6-5-7-10-20)40-32(46)48-33(2,3)4;1-2(3)4/h5-7,9-10,12-13,15,17,23-25,41H,8,11,14,16,18H2,1-4H3,(H,37,43)(H,38,45)(H,39,44)(H,40,46)(H4,34,35,36);1H3,(H,3,4)/t23-,24-,25-;/m0./s1 InChI key WGWZNYKOUXOZTC-NAGNLMCHSA-N Gene Information human ... TPSAB1(7177), TPSB2(64499), TPSD1(23430), TPSG1(25823)
Safety InformationRIDADR NONH for all modes of transport WGK Germany WGK 1 Flash Point F Not applicable Flash Point C Not applicable Узнать цену -
Tryptase, Human Lung
Enzyme Commission (EC) Number: 3.4.21.59 ( BRENDA | IUBMB )
Кат. номер 650366-1MG-M 650366-25UG-M 650366-25UGCN General descriptionNative tryptase from human lung. Tryptase is a serine protease stored in mast cell granules. A tetrameric enzyme composed of four non-covalently bound subunits. Each subunit is reported to contain one active site. Reported to upregulate neoangiogenesis in carcinogenesis of the uterine cortex. Tryptase is also an important mediator of allergic reactions that activates G-protein-coupled receptors through proteolysis, thus amplifying histamine release.
Native tryptase from human lung. Tryptase is a serine protease stored in mast cell granules. A tetrameric enzyme composed of four non-covalently bound subunits. Each subunit is reported to contain one active site. Tryptase is an important mediator of allergic reactions that activates G-protein-coupled receptors through proteolysis, thus amplifying histamine release.
Warning
Toxicity: Irritant (B)
Unit Definition
One unit is defined as the amount of enzyme that gives a change of 1 absorbance per min at 410 nm using N-benzoyl-Phe-Val-Arg-pNA as a substrate in 30 min at 25°C.
Physical form
In 1 M NaCl, 50 mM NaOAc, 50 µM heparin, pH 5.0.
Preparation Note
Prepared from tissue that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
Reconstitution
Following initial thaw, aliquot and freeze (-20°C).Other NotesBenitez-Bribiesca, L., et al. 2001. J. Histochem. Cytochem.49, 1061.
He, S., et al. 1998. J. Pharmacol. Exp. Ther. 286, 289.
Molino, M., et al. 1997. J. Biol. Chem. 272, 4043.
Schwartz, L.B., and Bradford, T.R. 1986. J. Biol. Chem. 261, 7372.Legal InformationCALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, GermanyПараметрыstorage conditions -20C form liquid Quality Level 100, specific activity 50 units/mg protein Торговая марка Calbiochem® storage condition OK to freeze, avoid repeated freeze/thaw cycles storage temp. 20°C Узнать цену -
TrypZean® bovine
CAS Number: 9002-07-7 Enzyme Commission (EC) Number: 3.4.21.4 ( BRENDA | IUBMB ) EC Number: 232-650-8 MDL number: MFCD04041188 NACRES: NA.54
Кат. номер T3568-10MG T3568-100MG General descriptionTrypZean® eliminates the introduction of animal source contaminants found in traditional bovine and porcine trypsins.ApplicationEliminates the introduction of animal source contaminants found in traditional bovine and porcine trypsins.
TrypZean® has been used in a study to assess the use of animal protein-free products for passaging adherent human adipose-derived stromal/stem cells. TrypZean® has also been used in a study to compare a recombinant trypsin with the porcine pancreatic extract on sperm used for the in vitro production of bovine embryos.
Packaging
10, 100 mg in glass bottle
Biochem/physiol Actions
For dissociation of cultured cells.
Preparation Note
Manufactured utilizing ProdiGene′s proprietary transgenic plant protein expression system.Legal InformationTrypzean is a registered trademark of ProdiGene, Inc.ПараметрыQuality Level 200 recombinant expressed in corn form lyophilized powder specific activity 3,350 units/mg solid (USP) UniProt accession no. Q29463, storage temp. 20°C Gene Information cow ... TRYP8(282603)
Safety Informationpictograms GHS07,GHS08 signalword Danger hcodes H315 - H319 - H334 - H335 pcodes P261 - P264 - P271 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 Target Organs Respiratory system Personal Protective Equipment dust mask type N95 (US),, Eyeshields,, Faceshields,, Gloves, RIDADR NONH for all modes of transport WGK Germany WGK 1 Узнать цену
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