Recombinant Bovine Fibroblast growth factor 2 (FGF2) (Active)

Function

Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Also acts as an integrin ligand which is required for FGF2 signaling (By similarity). Binds to integrin ITGAV:ITGB3 (By similarity). Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration (By similarity). Functions as a potent mitogen in vitro (By similarity). Can induce angiogenesis (By similarity). Mediates phosphorylation of ERK1/2 and thereby promotes retinal lens fiber differentiation (By similarity)

Subcellular Location

Secreted; Nucleus

Subunit

Monomer. Homodimer. Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Interacts with CSPG4, FGFBP1 and TEC. Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with FGFBP3. Interacts with integrin ITGAV:ITGB3; the interaction is required for FGF2 signaling. Interacts with SNORC (via the extracellular domain). Interacts with glypican GPC3

• Abraham J.A. et al. Nucleotide sequence of a bovine clone encoding the angiogenic protein, basic fibroblast growth factor. — Science (1986)
• Abraham J.A. et al. Human basic fibroblast growth factor: nucleotide sequence, genomic organization, and expression in mammalian cells. — Cold Spring Harb. Symp. Quant. Biol. (1986)
• Esch F. et al. Primary structure of bovine pituitary basic fibroblast growth factor (FGF) and comparison with the amino-terminal sequence of bovine brain acidic FGF. — Proc. Natl. Acad. Sci. U.S.A. (1985)
• Ueno N. et al. Isolation of an amino terminal extended form of basic fibroblast growth factor. — Biochem. Biophys. Res. Commun. (1986)
• Gospodarowicz D. et al. Isolation of fibroblast growth factor from bovine adrenal gland: physicochemical and biological characterization. — Endocrinology (1986)
• Bohlen P. et al. Isolation and partial molecular characterization of pituitary fibroblast growth factor. — Proc. Natl. Acad. Sci. U.S.A. (1984)
• Bertolini J. et al. Isolation, characterisation and tissue localisation of an N-terminal-truncated variant of fibroblast growth factor. — Mol. Cell. Endocrinol. (1987)
• Baird A. et al. Isolation and partial characterization of an endothelial cell growth factor from the bovine kidney: homology with basic fibroblast growth factor. — Regul. Pept. (1985)