Recombinant FGF1 protein (His tag)

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Recombinant Human Fibroblast Growth Factor 1 (FGF-1) Fragment (residues 16-155) is a highly purified, stable protein designed for advanced research applications. This 140-amino acid fragment retains key functional domains, offering a soluble and structurally defined unit ideal for investigating cell signaling, angiogenesis, and mitogenic activity in vitro.

Fibroblast Growth Factor 1 (FGF-1), also known as acidic fibroblast growth factor or endothelial cell growth factor, is a critical regulator of cell survival, division, differentiation, migration, and angiogenesis. It functions as a potent mitogen by binding to FGFR1 and integrins, such as ITGAV:ITGB3, in a heparin-dependent manner. This interaction triggers receptor dimerization, autophosphorylation, and activation of downstream signaling pathways, including MAPK/ERK and AKT, essential for cellular responses. FGF-1 is secreted via a non-classical pathway requiring Cu²⁺ ions and S100A13, and it can translocate to the cytosol and nucleus upon endocytosis, involving nuclear import machinery like KPNA1 and KPNB1. The provided fragment (residues 16-155) encompasses a stable, soluble domain optimized for structural and biochemical studies, enabling precise analysis of FGF-1's role in developmental and pathological processes.