Vascular endothelial growth factor receptor-1 (VEGFR-1, FLT-1) is a receptor tyrosine kinase belonging to the VEGFR family. VEGF is a key regulator of physiological angiogenesis and has also been implicated in pathological angiogenesis associated with tumors, intraocular neovascular disorders and other conditions. The biological effects of VEGF are mediated by VEGFR-1 and VEGFR-2. Both the two receptors have seven immunoglobulin-like repeats in the extracellular domain, a single transmembrane region and a tyrosine kinase domain. VEGFR-1 binds VEGFA, PIGF and VEGFB, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. Two isoforms of VEGFR-1 exist, a full-length transmembrane form and a short souble form (sVEGFR-1) consisting of only the extracellular ligand-binding domain.
Western Blot: HEK-293 Cells, 1:200-1:2000; IP:A549 Cells, 1:200-1:2000; IF: HeLa Cells, 1:10-1:100
Type: Primary
Antigen: VEGFR-1/FLT-1
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope:
Host: Rabbit
Isotype: IgG
Reactivity: Human, Mouse, Rat