FGF-1 Protein, Human (Biotinylated, His, Avi)

FGF-1 protein complexly regulates cell survival, division, angiogenesis, differentiation, and migration. As a potent mitogen, it acts as a ligand for FGFR1 and integrins. FGF-1 Protein, Human (Biotinylated, His, Avi) is the recombinant human-derived FGF-1 protein, expressed by E. coli, with N-His and N-Avi labeled tag.

FGF-1 Protein assumes a pivotal role in intricately regulating cell survival, division, angiogenesis, differentiation, and migration. Functioning as a potent mitogen in vitro, it acts as a ligand for FGFR1 and integrins. Binding to FGFR1, particularly in the presence of heparin, leads to FGFR1 dimerization and activation through sequential autophosphorylation on tyrosine residues. This activation serves as docking sites for interacting proteins, initiating several signaling cascades. Furthermore, FGF-1 Protein binds to integrin ITGAV:ITGB3, forming a ternary complex with integrin and FGFR1, crucial for FGF1 signaling. Inducing the phosphorylation and activation of FGFR1, FRS2, MAPK3/ERK1, MAPK1/ERK2, and AKT1, it demonstrates its involvement in diverse cellular processes. Additionally, FGF-1 Protein's ability to induce angiogenesis further underscores its multifaceted role. Interactions with FGFRs, integrins, and various proteins within complex networks highlight its intricate participation in cellular signaling pathways, emphasizing its significance in cell physiology.

Human

E. coli

N-Avi;N-8*His

P05230-1 (F16-D155)

2246

Full Length of Isoform-1 Mature Protein

FNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD

Approximately 20-24 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

Greater than 95% as determined by Bis-Tris PAGE.

<1 EU/μg, determined by LAL method.