Recombinant Human Fibroblast Growth Factor 1/FGF-1/FGFa (Phe16-Asp155)

Source: E. coli. MW :15.9kD. Recombinant Human Fibroblast growth factor 1 is produced by our E.coli expression system and the target gene encoding Phe16-Asp155 is expressed. FGF acidic, also known as ECGF, FGF-1and HBGF-1, is a non-glycosylated heparin binding growth factor that is expressed in the brain, kidney, retina, smooth muscle cells, bone matrix, osteoblasts, astrocytes and endothelial cells. It is a mitogenic peptide that is produced by multiple cell types and stimulates the proliferation of cells of mesodermal, ectodermal, and endodermal origin. Its association with heparan sulfate is a prerequisite for activation of FGF receptors. Internalized FGF acidic migrates to the nucleus where it is phosphorylated by nuclear PKC delta, exported to the cytosol, dephosphorylated, and degraded. Intracellular FGF acidic inhibits p53 activity and proapoptotic signaling. Protein function: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequential autophosphorylation on tyrosine residues which act as docking sites for interacting proteins, leading to the activation of several signaling cascades. Binds to integrin ITGAV:ITGB3. Its binding to integrin, subsequent ternary complex formation with integrin and FGFR1, and the recruitment of PTPN11 to the complex are essential for FGF1 signaling. Induces the phosphorylation and activation of FGFR1, FRS2, MAPK3/ERK1, MAPK1/ERK2 and AKT1 (PubMed:18441324, PubMed:20422052). Can induce angiogenesis (PubMed:23469107). [The UniProt Consortium]