Anti-VEGF Receptor 1, clone FLT1/658

1 mg/ml in sterile PBS, BSA free, sodium azide free. Three cell membrane receptor tyrosine kinases, VEGF receptor 1 (also designated Flt-1), VEGFR2 (also designated Flk-1) and Flt-4, putatively involved in the growth of endothelial cells, are characterized by the presence of seven immunoglobulin-like sequences in their extracellular domain. These receptors exhibit high degrees of sequence relatedness to each other as well as lesser degrees of relatedness to the class III receptors including CSF-1/Fms, PDGR, SLFR/Kit and Flt-3/Flk-2. Two members of this class, VEGF receptor 1 and 2, have been shown to represent high affinity receptors for vascular endothelial growth factors (VEGFs). On the basis of structural similarity to VEGF receptor 1 and 2, it has been speculated that Flt-4 might represent a third receptor for either VEGF or a VEGF-related ligand. Protein function: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, 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. May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). Has very high affinity for VEGFA and relatively low protein kinase activity, may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Likewise, isoforms lacking a transmembrane domain, such as isoform 2, isoform 3 and isoform 4, may function as decoy receptors for VEGFA. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC and YES1, and may also phosphorylate CBL. Isoform 1 phosphorylates PLCG. Promotes phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of PTK2/FAK1. Isoform 7 has a truncated kinase domain, it increases phosphorylation of SRC at 'Tyr-418' by unknown means and promotes tumor cell invasion. [The UniProt Consortium]