hFGF-b

hFGF-b
Human Fibroblast Growth Factor-basic
Recombinant, E. coli
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Fibroblast growth factor-basic (FGF-b, FGF-2) belongs to the 23 member FGF family. FGFs play major roles in development, wound healing, hematopoiesis, tumorigenesis, and angiogenisis. It is expressed mostly in tissues of mesoderm and neuroectoderm origin.

FGF-b exists in four molecular forms, three high molecular weight (21.5, 22, and 24 kDa), and one 18 kDa form. The higher molecular weight forms are mainly nucleus associated. The 18 kDa form, which lacks a signal sequence, is cytoplasmic or found at the cell surface.

FGF-b may be released from damaged cells or could be released by an exocytotic mechanism that is independent of the ER-Golgi pathway. Secreted FGF interacts with specific cell surface receptors. The FGF receptor family consists of four members: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. These receptors comprise a conserved tyrosine kinase domain, a transmembrane domain and an extracellular ligand binding domain. Binding of FGF-b to its receptor is regulated by heparan sulfate proteoglycans. FGF-b is implicated in many biological processes. It has been shown to induce endothelial cell proliferation, migration and angiogensis in vitro and in vivo, to stimulate myeloid progenitors, to stimulate stromal growth, to promote the release of endothelium from its connective tissue anchor (thus encouraging the entry of new vascular endothelium), to regulate oligodendrocyte progenitor proliferation and differentiation in culture, and to play a role in the autonomous growth of melanoma cells.

Neurotrophic Factors, Heparin-Binding Growth Factors.

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