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341595

Sigma-Aldrich

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

Sinónimos:

FGF-2, Basic, Human, Recombinant, E. coli, rhbFGF, Fibroblast Growth Factor, Basic, Human, Recombinant, E. coli

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About This Item

Número de CAS:
MDL number:
UNSPSC Code:
12352202

assay

≥97% (SDS-PAGE)

Quality Level

form

lyophilized

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

impurities

≤1 EU/μg Endotoxin (EU/μg FGF)

shipped in

ambient

storage temp.

−70°C

General description

Recombinant, 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.
Recombinant, 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.

Biochem/physiol Actions

ED₅₀ = 100-250 pg/ml as monitored in a mitogenic assay by measuring FGF basic-dependent ³H-thymidine incorporation in quiescent NR6R/3T3 fibroblasts

Warning

Toxicity: Standard Handling (A)

Physical form

Lyophilized from sterile-filtered 20 mM Tris-HCl, 1 M NaCl, 50 µg BSA/1 µg cytokine, pH 7.0.

Reconstitution

Following 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.
Reconstitute to a concentration ≥10 µg/ml with sterile PBS containing 1 mM DTT and ≥0.1% HSA or BSA.

Other Notes

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. Cancer72, 2253.
Mignatti, P., et al. 1992. J. Cell Physiol.151, 81.
Mignatti, P., et al. 1991. Proc. Natl. Acad. Sci. USA88, 11007.
Baird, A., and Klagsbrun, M. 1991. Cancer Cells3, 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.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3


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S Rogelj et al.
Journal of cellular biochemistry, 39(1), 13-23 (1989-01-01)
Basic fibroblast growth factor (bFGF) is found in a variety of cells and tissues. We have previously shown that bFGF is a transforming growth factor, but only when fused to a signal peptide (sp-bFGF). Cells expressing the native bFGF are
P Mignatti et al.
Proceedings of the National Academy of Sciences of the United States of America, 88(24), 11007-11011 (1991-12-15)
Basic fibroblast growth factor (bFGF), a protein with angiogenic, mitogenic, and chemotactic properties, lacks a signal sequence and is not secreted via the classical secretory pathway. However, the growth factor is known to act extracellularly. Since no defined mechanism for
Biological activities of fibroblast growth factors.
D Gospodarowicz
Annals of the New York Academy of Sciences, 638, 1-8 (1991-01-01)
Expression and activation of the K-fgf oncogene.
C Basilico et al.
Annals of the New York Academy of Sciences, 567, 95-103 (1989-01-01)
N S Gibran et al.
The Journal of surgical research, 56(3), 226-234 (1994-03-01)
The role of endogenous growth factors in normal wound healing is not clear. Most of the data on growth factors in healing wounds have been obtained from the application of recombinant exogenous growth factors to animal and human wounds. We

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