Anti-VEGF Receptor 2/Kdr Antibody Picoband® Fluoro488 Conjugated

KDR (Kinase Insert Domain Receptor), also known as FLK1, VEGFR or VEGFR2, is a VEGF receptor. KDR is the human gene encoding it. 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. Flk1 is the mouse homolog of KDR.

Vascular endothelial growth factor receptor 2; VEGFR-2; Fetal liver kinase 1; FLK-1; Kinase NYK; Protein-tyrosine kinase receptor flk-1; CD309; Kdr; Flk-1; Flk1

Expressed in endothelial cells (at protein level) . Detected in embryonic endothelial cells, as well as hematopoietic stem and progenitor cells. Detected in vascular endothelium. Expressed at high levels in adult heart, lung, kidney, brain and skeletal muscle, but is also expressed at lower levels in most other adult tissues.

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, such as isoform 2, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as a negative regulator of VEGFA- and VEGFC- mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and by 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.

1. Matthews, W., Jordan, C. T., Gavin, M., Jenkins, N. A., Copeland, N. G., Lemischka, I. R. A receptor tyrosine kinase cDNA isolated from a population of enriched primitive hematopoietic cells and exhibiting close genetic linkage to c-kit. Proc. Nat. Acad. Sci. 88: 9026-9030, 1991. 2. Plate, K. H., Breier, G., Millauer, B., Ullrich, A., Risau, W. Up-regulation of vascular endothelial growth factor and its cognate receptors in a rat glioma model of tumor angiogenesis. Cancer Res. 53: 5822-5827, 1993. 3. Sait, S. N. J., Dougher-Vermazen, M., Shows, T. B., Terman, B. I. The kinase insert domain receptor gene (KDR) has been relocated to chromosome 4q11-q12. Cytogenet. Cell Genet. 70: 145-146, 1995.