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341595 FGF-2, Basic, Human, Recombinant, E. coli

341595
  
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Áttekintés

Replacement Information

Kulcsspecifikációk táblázata

Purity
≥97% by SDS-PAGE
Description
OverviewRecombinant, human basic fibroblast growth factor expressed in E. coli. Potent mitogen for bone cells. Inhibits DNA synthesis and alkaline phosphatase activity in rat osteosarcoma cell lines. Has been implicated in the development of Kaposi sarcoma in vitro. Inhibits inducible NOS in bovine retinal pigmented epithelial cells.
Catalogue Number341595
Brand Family Calbiochem®
SynonymsrhbFGF, Fibroblast Growth Factor, Basic, Human, Recombinant, E. coli
References
ReferencesGoureau, O., et al. 1995. Eur. J. Biochem. 230, 1046.
Gibran, N.S., et al. 1994. J. Surg. Res. 56, 226.
Li, J.J., et al. 1993. Cancer 72, 2253.
Mignatti, P., et al. 1992. J. Cell Physiol. 151, 81.
Mignatti, P., et al. 1991. Proc. Natl. Acad. Sci. USA 88, 11007.
Baird, A., and Klagsbrun, M. 1991. Cancer Cells 3, 239.
Gospodarowicz, D. 1991. Ann. NY Acad. Sci. 638, 1.
Basilico, C., et al. 1989. Ann. NY Acad. Sci. 567, 95.
Burgess, W.H., and Maciag, T. 1989. Annu. Rev. Biochem. 58, 575.
Rogelj, S., et al. 1989. J. Cell. Biochem. 39, 13.
Rizzino, A., et al. 1988. Cancer Res. 48, 4266.
Abraham, J.A., et al. 1986. EMBO J. 5, 2523.
Product Information
CAS number106096-93-9
FormLyophilized
FormulationLyophilized from sterile-filtered 20 mM Tris-HCl, 1 M NaCl, 50 µg BSA/1 µg cytokine, pH 7.0.
Quality LevelMQ100
Applications
Biological Information
Biological activityED₅₀ = 100-250 pg/ml as monitored in a mitogenic assay by measuring FGF basic-dependent ³H-thymidine incorporation in quiescent NR6R/3T3 fibroblasts
Purity≥97% by SDS-PAGE
Physicochemical Information
ContaminantsEndotoxin: ≤1 EU/µg FGF
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
RTECSLK3641325
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Standard Handling
Storage ≤ -70°C
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-70°C) for long term storage or refrigerate (4°C) for short term storage. Avoid freeze/thaw cycles of solutions. Stock solutions are stable for up to 1 month at 4°C or for up to 6 months at -70°C.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Katalógusszám GTIN
341595 0

Documentation

FGF-2, Basic, Human, Recombinant, E. coli MSDS

Title

Safety Data Sheet (SDS) 

FGF-2, Basic, Human, Recombinant, E. coli Certificates of Analysis

TitleLot Number
341595

References

Hivatkozások áttekintése
Goureau, O., et al. 1995. Eur. J. Biochem. 230, 1046.
Gibran, N.S., et al. 1994. J. Surg. Res. 56, 226.
Li, J.J., et al. 1993. Cancer 72, 2253.
Mignatti, P., et al. 1992. J. Cell Physiol. 151, 81.
Mignatti, P., et al. 1991. Proc. Natl. Acad. Sci. USA 88, 11007.
Baird, A., and Klagsbrun, M. 1991. Cancer Cells 3, 239.
Gospodarowicz, D. 1991. Ann. NY Acad. Sci. 638, 1.
Basilico, C., et al. 1989. Ann. NY Acad. Sci. 567, 95.
Burgess, W.H., and Maciag, T. 1989. Annu. Rev. Biochem. 58, 575.
Rogelj, S., et al. 1989. J. Cell. Biochem. 39, 13.
Rizzino, A., et al. 1988. Cancer Res. 48, 4266.
Abraham, J.A., et al. 1986. EMBO J. 5, 2523.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision02-May-2008 RFH
SynonymsrhbFGF, Fibroblast Growth Factor, Basic, Human, Recombinant, E. coli
DescriptionRecombinant, human basic fibroblast growth factor expressed in E. coli. A member of the FGF family of mitogenic peptides, comprised of seven related proteins showing 35-55% amino acid conservation within the family and 55% similarity with acidic FGF. Found in neuronal tissue (hippocampus, brain stem, peripheral ganglia, and the isocortex), pituitary, adrenal cortex, corpus luteum, and placenta. Some of the biological activities attributed to basic FGF include: mitogenic activity in vitro for cells of meso- and neuroectodermal origin (i.e. fibroblasts, endothelial cells, astrocytes, oligodendrocytes, neuroblasts, keratinocytes, bovine epithelial lens cells, osteoblasts, smooth muscle cells, and melanocytes); role in wound healing; induction of neuron differentiation, survival, and regeneration; chemoattractant effect and mitogenic activity in vitro for endothelial cells and angiogenic activity in vivo; role in tumor neovascularization. Inhibits DNA synthesis and alkaline phosphatase activity in rat osteosarcoma cell lines. Has been implicated in the development of Kaposi sarcoma in vitro. Inhibits iNOS in bovine retinal pigmented epithelial cells. Binding of FGF to heparin or cell surface heparin sulfate proteoglycans is necessary for FGF binding to its high affinity receptors. Basic and acidic FGF appear to bind to the same high affinity receptors and show a similar range of biological activities.
FormLyophilized
FormulationLyophilized from sterile-filtered 20 mM Tris-HCl, 1 M NaCl, 50 µg BSA/1 µg cytokine, pH 7.0.
CAS number106096-93-9
RTECSLK3641325
Purity≥97% by SDS-PAGE
ContaminantsEndotoxin: ≤1 EU/µg FGF
Biological activityED₅₀ = 100-250 pg/ml as monitored in a mitogenic assay by measuring FGF basic-dependent ³H-thymidine incorporation in quiescent NR6R/3T3 fibroblasts
SolubilityReconstitute to a concentration ≥10 µg/ml with sterile PBS containing 1 mM DTT and ≥0.1% HSA or BSA.
Storage ≤ -70°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-70°C) for long term storage or refrigerate (4°C) for short term storage. Avoid freeze/thaw cycles of solutions. Stock solutions are stable for up to 1 month at 4°C or for up to 6 months at -70°C.
Toxicity Standard Handling
Merck USA index14, 4072
ReferencesGoureau, O., et al. 1995. Eur. J. Biochem. 230, 1046.
Gibran, N.S., et al. 1994. J. Surg. Res. 56, 226.
Li, J.J., et al. 1993. Cancer 72, 2253.
Mignatti, P., et al. 1992. J. Cell Physiol. 151, 81.
Mignatti, P., et al. 1991. Proc. Natl. Acad. Sci. USA 88, 11007.
Baird, A., and Klagsbrun, M. 1991. Cancer Cells 3, 239.
Gospodarowicz, D. 1991. Ann. NY Acad. Sci. 638, 1.
Basilico, C., et al. 1989. Ann. NY Acad. Sci. 567, 95.
Burgess, W.H., and Maciag, T. 1989. Annu. Rev. Biochem. 58, 575.
Rogelj, S., et al. 1989. J. Cell. Biochem. 39, 13.
Rizzino, A., et al. 1988. Cancer Res. 48, 4266.
Abraham, J.A., et al. 1986. EMBO J. 5, 2523.