VEGFR-1 Protein, Human (756a.a, HEK293, His)

The VEGFR-1 protein is a tyrosine protein kinase that acts as a cell surface receptor for VEGFA, VEGFB, and PGF. It plays a crucial role in embryonic vasculature development, regulation of angiogenesis, cell survival, migration, macrophage function, chemotaxis, and cancer cell invasion. VEGFR-1 Protein, Human (756a.a, HEK293, His) is the recombinant human-derived VEGFR-1 protein, expressed by HEK293 , with C-His labeled tag.

VEGFR-1 Protein is a tyrosine-protein kinase that serves as a cell-surface receptor for VEGFA, VEGFB, and PGF. It plays a crucial role in various biological processes, including embryonic vasculature development, angiogenesis regulation, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. Additionally, VEGFR-1 acts as a positive regulator of postnatal retinal hyaloid vessel regression and may function as a negative regulator of embryonic angiogenesis by inhibiting excessive endothelial cell proliferation. In adulthood, it promotes endothelial cell proliferation, survival, and angiogenesis, although its proliferative effects appear to be cell-type specific. VEGFR-1 has a high affinity for VEGFA and acts as a negative regulator of its signaling by limiting the availability of free VEGFA and preventing its binding to KDR. It modulates KDR signaling by forming heterodimers with KDR. Ligand binding to VEGFR-1 activates several signaling cascades, including PLCG, MAPK1/ERK2, MAPK3/ERK1, AKT1, and PI3K pathways. VEGFR-1 also phosphorylates SRC, YES1, CBL, AKT1, PTK2/FAK1, and PLCG.

Human

HEK293

C-His

P17948-1 (S27-N756)

2321  [NCBI]

110-120 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.