Anti-VEGFR2 Rabbit (Clone RM515)

VEGFR2, also known as kinase insert domain receptor (KDR), is a receptor tyrosine kinase that has roles in vascular permeability, cell proliferation and survival, and angiogenesis. It is composed of an N-terminal extracellular ligand-binding domain, which contains seven immunoglobulin-like (Ig-like) domains, a transmembrane domain, and an intracellular tyrosine kinase domain, which is subject to phosphorylation and contains a kinase insert domain and the C-terminal domain. VEGFR2 is expressed primarily in vascular and lymphatic endothelial cells, where it is bound by the growth factors VEGF-A, VEGF-C, and VEGF-D. Upon ligand binding, VEGFR2 forms homodimers or heterodimers with VEGFR1 or VEGFR3, resulting in VEGFR2 phosphorylation and activation of a variety of intracellular signaling pathways, including the ERK/MAPK pathway, to promote endothelial cell survival, proliferation, and migration. VEGFR2 also exists in a soluble form that is generated by alternative splicing of the KDR pre-mRNA or proteolytic shedding and decreases angiogenesis by functioning as a decoy receptor for VEGF-A. VEGFR2 expression is increased in the tumor vasculature of patients with a variety of solid tumors, including colorectal, lung, pancreatic, and breast cancer. Cayman's VEGFR2 Rabbit Monoclonal Antibody (Clone RM515) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.. Cross reactivity: (+) VEGFR2: . (+) Human: .. 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]