Anti-VEGFR2/KDR Monoclonal Antibody

VEGF, a homodimeric glycoprotein of relative molecular mass 45,000, is the only mitogen that specifically acts on endothelial cells. The importance of VEGF and its receptor system in tumor growth and intervention in this system may provide promising approaches to cancer therapy. VEGF receptor 2 is a member of a receptor tyrosine kinase family. Like other growth factor receptors, upon ligand binding VEGF receptor 2 dimerises and is autophosphorylated on multiple tyrosine residues.

Angiogenesis, Cancer, Cancer Metabolism, Cardiovascular, Growth Factors, Growth Factors/Hormones, Hematopoietic Progenitors, Host-Virus Interaction, Interspecies Interaction, Invasion/Microenvironment, Metabolism, Metabolism Processes, Microbiology, Oncoproteins, Oncoproteins/Suppressors, Pathways and Processes, Protein Phosphorylation, Receptor Tyrosine Kinases, Response To Hypoxia, Signal Transduction, Stem Cells, Surface Molecules, Tyrosine Kinases

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 may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. 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 (By similarity) . .

1. Folkman, J. : Angiogenesis in cancer, vascular, rheumatoid and other disease. Nature Med. 1: 27-31, 1995. 2. Millauer, B.; Shawver, L. K.; Plate, K. H.; Risau, W.; Ullrich, A. : Glioblastoma growth inhibited in vivo by a dominant-negative Flk-1 mutant. Nature 367: 576-579, 1994.

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.

Cell membrane ; Single-pass type I membrane protein . Cytoplasm . Nucleus . Cytoplasmic vesicle . Early endosome . Cell junction . Endoplasmic reticulum . Detected on caveolae-enriched lipid rafts at the cell surface. Is recycled from the plasma membrane to endosomes and back again. Phosphorylation triggered by VEGFA binding promotes internalization and subsequent degradation. VEGFA binding triggers internalization and translocation to the nucleus. Localized with RAP1A at cell-cell junctions. Colocalizes with ERN1 and XBP1 in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF) -dependent manner (By similarity) . .