VEGFR-1 Protein, Mouse (HEK293, His)

VEGFR-1, a tyrosine-protein kinase, acts as a pivotal cell-surface receptor for VEGFA, VEGFB, and PGF, playing indispensable roles in embryonic vasculature development, angiogenesis regulation, cell survival, migration, macrophage function, chemotaxis, and cancer cell invasion. It functions as a positive regulator in the regression of postnatal retinal hyaloid vessels. While potentially acting as a negative regulator of embryonic angiogenesis by curbing excessive endothelial cell proliferation, VEGFR-1 also exhibits cell-type-specific promotion of proliferation, survival, and angiogenesis in adulthood, especially in response to PGF. With a high affinity for VEGFA, it modulates KDR signaling through heterodimer formation. Acting as a potential negative regulator of VEGFA signaling, it limits free VEGFA, hindering its binding to KDR. Ligand binding triggers various signaling cascades, including PLCG activation, leading to diacylglycerol and inositol 1,4,5-trisphosphate production, as well as protein kinase C activation. Additionally, VEGFR-1 mediates the phosphorylation of PIK3R1, initiating the phosphatidylinositol 3-kinase pathway, and activates MAPK1/ERK2, MAPK3/ERK1, and AKT1 signaling pathways. It also phosphorylates SRC, YES1, PLCG, and potentially CBL, facilitating the phosphorylation of AKT1 and PTK2/FAK1.