341595
FGF-2, Basic, Human, Recombinant, E. coli
别名:
FGF-2, Basic, Human, Recombinant, E. coli, rhbFGF, Fibroblast Growth Factor, Basic, Human, Recombinant, E. coli
方案
≥97% (SDS-PAGE)
质量水平
表单
lyophilized
制造商/商品名称
Calbiochem®
储存条件
OK to freeze
杂质
≤1 EU/μg Endotoxin (EU/μg FGF)
运输
ambient
储存温度
−70°C
一般描述
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.
生化/生理作用
ED₅₀ = 100-250 pg/ml as monitored in a mitogenic assay by measuring FGF basic-dependent ³H-thymidine incorporation in quiescent NR6R/3T3 fibroblasts
外形
Lyophilized from sterile-filtered 20 mM Tris-HCl, 1 M NaCl, 50 µg BSA/1 µg cytokine, pH 7.0.
制备说明
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.
其他说明
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.
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.
法律信息
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
免责声明
Toxicity: Standard Handling (A)
储存分类代码
11 - Combustible Solids
WGK
WGK 3
法规信息
新产品
此项目有
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)
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
O Goureau et al.
European journal of biochemistry, 230(3), 1046-1052 (1995-06-15)
Bovine retinal pigmented epithelial cells (RPE cells), after activation with interferon gamma (IFN gamma) and lipopolysaccharide (LPS), express an inducible nitric oxide (NO) synthase. This activity can be inhibited by the fibroblast growth factors (FGF), FGF-1 (acidic FGF) and FGF-2
P Mignatti et al.
Journal of cellular physiology, 151(1), 81-93 (1992-04-01)
Basic fibroblast growth factor (bFGF) modulates functions of a variety of cell types. Whereas bFGF is known to act extracellularly, the protein lacks a transient signal peptide. No defined mechanism for bFGF secretion has been characterized besides release from dead
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