Mouse Anti-FGF1 Recombinant Antibody (CBXF-0532) (CBMAB-F0857-CQ)

Fibroblast Growth Factor 1

The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Multiple alternatively spliced variants encoding different isoforms have been described.

Fibroblast Growth Factor 1; Heparin-Binding Growth Factor 1; Endothelial Cell Growth Factor, Alpha; Endothelial Cell Growth Factor, Beta; Fibroblast Growth Factor 1 (Acidic); HBGF-1; FGF-1; AFGF; FGFA; ECGF;

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).

Activation of MAPK activity Source: UniProtKB
Activation of protein kinase B activity Source: UniProtKB
Anatomical structure morphogenesis Source: ProtInc
Angiogenesis Source: UniProtKB-KW
Animal organ morphogenesis Source: GO_Central
Branch elongation involved in ureteric bud branching Source: UniProtKB
Cell differentiation Source: GO_Central
Cellular response to heat Source: UniProtKB
Fibroblast growth factor receptor signaling pathway Source: UniProtKB
Lung development Source: GO_Central
Mesonephric epithelium development Source: UniProtKB
Multicellular organism development Source: ProtInc
Organ induction Source: Ensembl
Positive regulation of angiogenesis Source: UniProtKB
Positive regulation of cell division Source: UniProtKB
Positive regulation of cell migration Source: UniProtKB
Positive regulation of cell population proliferation Source: UniProtKB
Positive regulation of cholesterol biosynthetic process Source: BHF-UCL
Positive regulation of endothelial cell migration Source: UniProtKB
Positive regulation of epithelial cell proliferation Source: GO_Central
Positive regulation of gene expression Source: GO_Central
Positive regulation of hepatocyte proliferation Source: Ensembl
Positive regulation of intracellular signal transduction Source: BHF-UCL
Positive regulation of MAP kinase activity Source: UniProtKB
Positive regulation of protein phosphorylation Source: GO_Central
Positive regulation of sprouting angiogenesis Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: BHF-UCL
Regulation of cell migration Source: GO_Central
Regulation of endothelial cell chemotaxis to fibroblast growth factor Source: UniProtKB
Regulation of endothelial tube morphogenesis Source: UniProtKB
Signal transduction Source: ProtInc
Wound healing Source: UniProtKB

Secreted; Nucleus; Cytoplasm; Cytosol; Cell cortex. Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu2+ ions and S100A13. Secreted in a complex with SYT1 (By similarity). Binding of exogenous FGF1 to FGFR facilitates endocytosis followed by translocation of FGF1 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as LRRC59.

In the nucleus, phosphorylated by PKC/PRKCD.