Anti-KDR / Kinase Insert Domain Receptor

0.5mg/ml if reconstituted with 0.2ml sterile DI water. KDR (Kinase Insert Domain Receptor), also known as FLK1, VEGFR or VEGFR2, is a VEGF receptor. KDR is the human gene encoding it. Sait et al. (1995) likewise corrected the assignment to chromosome 4q11-q12 to the same region occupied also by PDGFRA and KIT, thus indicating the location of a cluster of receptor tyrosine kinase genes. Vascular endothelial growth factor (VEGF) is the only mitogen that specifically acts on endothelial cells. Its expression is upregulated by hypoxia, and its cell-surface receptor, known as fetal liver kinase-1 (Flk1) in mouse, is exclusively expressed in endothelial cells (Plate et al., 1993). Flk1 is the mouse homolog of KDR (Matthews et al., 1991). Protein function: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC. [The UniProt Consortium]