Growth Factors & Cytokines Roche
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BM-Cyclin 10799050001
General descriptionBM-Cyclin is a combination of two antibiotics, namely tiamulin and minocycline, both of which prevent protein synthesis.SpecificitySensitive Organisms: Mycoplasmas and bacteria- BM Cyclin was found to effectively eliminate Acholesplasma laidlawii,
- Mycoplasma arginini,
- Mycoplasma hyorhinis, and
- Mycoplasma orale
Note: These mycoplasma strains account for more than 85% of the contaminations in animal cell cultures.ApplicationBM-Cyclin is used for the elimination of mycoplasma from infected cell cultures without obvious marked cytotoxic side effects.PackagingSet of two different antibioticsPhysical formVial 1 (Tiamulin-hydrogenfumarat): clear, colorless solution after reconstitution
Vial 2 (Minocyclinhydrochloride): clear, yellow solution after reconstitutionPreparation NoteWorking concentration: 10µg/ml pleuromutilin derivative (BM-cyclin 1), 5µg/ml tetracycline derivative (BM-cyclin 2).
Note: These concentrations do not affect the growth of most cells. Lower concentrations may be used for sensitive cell lines.
For hybridomas decrease concentration of BM-Cyclin by 50%.
Preparation of DAPI Working Solution
Dilute the stock solution with methanol to a final concentration of 1µg/ml.
Working solution: Preparation of Stock Solution
Dissolve content of BM Cyclin 1 and BM Cyclin 2 in 10ml sterile PBS or water.
Note: These are 250x concentrated stock solutions and can be stored at -15 to -25°C for at least 6 months.Preparation of DAPI Stock Solution
Dissolve DAPI in water to a final concentration of 1 to 5mg/ml.
Note: Do not use any buffers.
This stock solution can be stored at -15 to -25°C. It is recommended to prepare appropriate aliquots.
Storage conditions (working solution): -15 to -25°C
Reconstituted stable at -15 to -25°C for at least 6 months.Other NotesFor life science research only. Not for use in diagnostic procedures.ПараметрыQuality Level 100 form lyophilized packaging pkg of 37.5 mg (for 2 x 2.5 l medium) Торговая марка Roche Mode of action protein synthesis | interferes antibiotic activity spectrum mycoplasma shipped in wet ice storage temp. 2-8°C
Safety InformationPictograms GHS07 Signal Word Warning Hazard Statements H302 - H315 - H319 - H335 Precautionary Statements P261 - P264 - P280 - P304 + P340 + P312 - P337 + P313 - P403 + P233 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 -
Epidermal Growth Factor, human (hEGF) 11376454001
General descriptionRecombinant Epidermal Growth Factor, human (hEGF), is produced in E. coli and purified by standard chromatographic techniques. It is a 100µg white lyophilizate, filtered through 0.2µm pore size membrane, recombinant from E. coli.
Epidermal growth factor (EGF) is a small mitogenic polypeptide which is present in many mammalian species and is distributed throughout a wide number of tissues and body fluids EGF is produced in the tubular cells of the submaxillary gland of the mouse, in the acinar cells of the human submaxillary gland, and in the human duodenal glands.
Human EGF is identical to -urogastrone, a polypeptide which was recognized and isolated on the basis of its ability to inhibit gastric acid secretion. 37 amino acids of the 53 amino acids comprising the longer urogastrone (human EGF) and mouse EGF are common to both peptides (70% homology) and the three disulfide bonds are formed in the same relative positions. The biological activity of human EGF is similar to that of mouse EGF. The cellular receptor for EGF is the best understood growth factor receptor. The oncogene v-erbB codes for a product homologous to a portion of the EGF receptor in which the EGF-binding domain has been deleted. Evidence exists suggesting that this truncation of the EGF receptor may lead to constitutive activation without requirement for ligand binding.
EGF stimulates the proliferation and differentiation of awide variety of cells of ectodermal and mesodermal origin (e.g., fibroblasts, glial cells, keratinocytes, epithelial cells, endothelial cells, chondrocytes). EGF is a constituent of many serum-free media formulations for a variety of cells.
Specificity
Species Specificity: Human EGF is effective on human and mouse cells.
Specific activity: <0.5 ng/ml, at least the same specific activity (EC50) compared to the indicated standard is guaranteed.ApplicationEpidermal growth factor (EGF) stimulates the proliferation and differentiation of a wide variety of cells of ectodermal and mesodermal origin, and is a constituent of many serum-free media formulations. It has been used in the cell differentiation assay.
Sequence
The primary structure of recombinant, human EGF (one polypeptide chain, 54 amino acids) is identical to that of human, natural EGF (β-urogastrone) (53 amino acids), however, recombinant EGF has an additional methionine at the amino-terminus.
Chain Length 54 AA
Unit Definition
Unit Conversion: 1 BM unit = 3.25 NBSB units (natural IL-2)1 BM unit = 3.25 NBSB units (natural IL-2)
Unit Definition: EC50 defintion: The concentration of hEGF that is required to support half-maximal stimulation of cell proliferation (MTT cleavage) with MK cells.
Physical form
White lyophilizate, filtered through 0.2 μm pore size membrane
Preparation Note
Working concentration: 0.5 to 20 ng/ml
Human EGF exerts its biological activity in the concentration range of 0.5 to 20 ng/ml. Recommended concentration for serum-free cell culture is 1 to 10 ng/ml
Working solution: In sterile water (final concentration: 500 µg/ml), further dilution with medium or PBS (phosphate buffered saline) containing 1 mg/ml BSA (bovine serum albumin), or 1 to 10% serum.
Storage conditions (working solution): -15 to -25 °C
It is recommended to store the reconstituted solution in aliquots at -15 to -25 °C.
Note: Avoid repeated freezing and thawing.Other NotesFor life science research only. Not for use in diagnostic procedures.ПараметрыQuality Level 100 biological source human recombinant expressed in E. coli assay >95% (HPLC) form lyophilized potency <0.5 ng/mL EC50 mol wt 6200 Da packaging pkg of 100 µg Торговая марка Roche storage condition avoid repeated freeze/thaw cycles color white UniProt accession no. Q6QBS2, shipped in dry ice storage temp. 20°C Gene Information human ... EGF(1950)
Safety InformationRIDADR NONH for all modes of transport WGK Germany WGK 1 Flash Point F does not flash Flash Point C does not flash Узнать цену -
Erythropoietin, human (hEPO) 11120166001
General descriptionRecombinant, Erythropoietin, human (hEPO), is produced in CHO cells (chinese hamster ovary) and purified by standard chromatographic techniques. The glycoprotein encoded by erythropoietin (EPO) is synthesized in kidneys. It is the principal hormone that has a short half-life. Cells responsive to EPO have been identified in adult bone marrow, fetal liver, or adult spleen.
Detection of digoxigenin-labeled nucleic acids by enzyme immunoassay and enzyme-catalyzed color reaction. We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product is designed as a safer chemical. The DIG System was established as a sensitive and cost-effective alternative to using radioactivity for the labeling and detection of nucleic acids. There are many available publications that prove the versatility of the DIG System, so use of radio-labeling is no longer the only option for labeling of DNA for hybridization.
Specificity
Human Erythropoietin (hEPO) is effective on mouse and human cells.ApplicationErythropoietin (EPO) is a glycoprotein which stimulates proliferation and differentiation of erythroid precursor cells (CFU-E, BFU-E) to more mature erythrocytes.
Biochem/physiol Actions
Erythropoietin (EPO) controls the synthesis of RBCs (red blood cells) by inducing the proliferation and differentiation of erythroid precursor cells. As it induces erythropoiesis, EPO can be used to treat anemia of cancer patients.
Sequence
One polypeptide chain (166 amino acids), glycosylated, identical to natural hEPO. The carbohydrate structure of recombinant EPO isolated from CHO cells is very similar to that of natural EPO.
Unit Definition
EC50 definition: The amount of hEPO that is required to produce equivalent [3H]-thymidine incorporation into spleen cells from phenylhydrazine-treated mice to that expressed by 1 unit of the WHO-EPO reference standard (2nd IRP) (1 unit equals 10 ng).
Physical form
Solution, filtered through 0.2 μm pore size membrane.
Preparation Note
Working solution: Dilute the concentrated EPO solution (250 U/ml) with PBS or culture medium containing 1 mg/ml (0.1%) BSA (or HSA) or 1 to 10% serum.
Storage conditions (working solution): -15 to -25 °C
Store the solution in aliquots at -15 to -25 °C
Note: Avoid repeated freezing and thawingOther NotesFor life science research only. Not for use in diagnostic procedures.ПараметрыQuality Level 100 biological source human recombinant expressed in CHO cells Hamster assay >98% (HPLC and SDS-PAGE) form solution packaging pkg of 250 U (2.5 µg, 1 ml) Торговая марка Roche storage condition avoid repeated freeze/thaw cycles impurities <1 EU/µgtested (LAL test) UniProt accession no. P01588, storage temp. 20°C Gene Information human ... EPO(2056)
Safety InformationRIDADR NONH for all modes of transport WGK Germany nwg Flash Point F No data available Flash Point C No data available Узнать цену -
Interleukin-6, human (hIL-6) 11138600001
General descriptionInterleukin-6, human (hIL-6), is produced in E. coli and purified by standard chromatographic techniques.
Specificity
Recombinant IL-6, human is effective on mouse and human cells.
IL-6, a 26 kD protein, also known as B-cell stimulatory factor 2 (BSF-2, BCDF), interferon-2 (IFN-2), hybridoma/plasmacytoma growth factor (H(P)GF), and hepatocyte-stimulating factor is produced by many cell types (e.g., T-cells, monocytes, fibroblasts, endothelial cells). IL-6 induces the terminal maturation of activated B-cells into antibody-producing cells (B-cell differentiation activity. The hepatic acute phase response is induced by IL-6 (hepatocyte-stimulating activity). It was shown that IL-6 and IL-3 act synergistically to support the proliferation of hematopoietic stem cells (hemapoietic activity), however, IL-6 does not have antiviral activity, although it has been called IFN-2. High affinity receptors for IL-6 are found on many cell types.ApplicationRecombinant IL-6, human, is a growth factor for murine and human B-cells. It can be used to replace feeder cells in the preparation of murine and human hybridomas.
Biochem/physiol Actions
Interleukin-6 participates in several pleiotropic functions in various types of cells through its specific receptor (IL-6-R). It has been suggested that interleukin-6 may participate in the interaction between neuroendocrine and immune system by activating adrenocorticotropic hormone secretion. It has also been reported that IL-6 stimulates the bonding of receptor (IL-6-R) with a non-ligand-binding membrane glycoprotein, gp130.
Quality
Purity: 95% pure as determined by HPLC or SDS-PAGE [Endotoxin level: <0.1 EU/µg (LAL-test), <10 EU/ml (LAL-test).
Note: 1 EU corresponds to 0.1 ng
Sequence
Chain Length 184 AA
The primary structure of recombinant human IL-6 is identical to that of natural human IL-6 (one polypeptide chain, 184 amino acids), however, it contains an altered sequence within the first 15 amino-terminal amino acids.
Unit Definition
EC50 definition: The amount of hIL-6 that is required to support half-maximal stimulation of cell proliferation (MTT cleavage) with 7TD1 cells (1 unit equals <0.01 ng).
Physical form
Solution, filtered through 0.2 μm pore size membrane.
Preparation Note
Working concentration: 10 to 100 U/ml (0.1 1 ng/ml)
10 to 100 U/ml (0.1 to 1 ng/ml)
A concentration of 100 U/ml (1 ng/ml) is recommended for the preparation of B-cell hybridomas
Working solution: Dilute the concentrated IL-6 solution (200,000 U/ml) with PBS or culture medium containing 1 mg/ml BSA [or HSA (human serum albumin)] or 1 to 10% serum.
Storage conditions (working solution): -15 to -25 °C
Store the solution in aliquots at -15 to -25 °C.
Note: Avoid repeated freezing and thawing.
Reconstitution
Dilute the concentrated IL-6 solution (200,000 U/ml) with PBS or culture medium containing 1 mg/ml BSA [or HSA (human serum albumin)] or 1 to 10% serum.
Analysis Note
Specific activity/EC50: >1 x 108 U/mg, <0.01 ng/ml (hIL-6, NIBSC, interim standard, 88/514), at least the same specific activity (EC50) compared to the indicated standard is guaranteed.Other NotesFor life science research only. Not for use in diagnostic procedures.ПараметрыQuality Level 100 biological source human recombinant expressed in E. coli assay >98% (SDS-PAGE) form solution potency <0.01 ng/mL EC50 mol wt 20,600 Da packaging pkg of 200,000 U (2 µg, 1 ml) Торговая марка Roche storage condition avoid repeated freeze/thaw cycles impurities <0.1 EU/µgtested (LAL test) UniProt accession no. P05231, shipped in dry ice storage temp. 20°C Gene Information human ... IL6(3569)
Safety InformationRIDADR NONH for all modes of transport WGK Germany nwg Flash Point F does not flash Flash Point C does not flash Узнать цену
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