ELISA/assay

Mouse VEGFR2/KDR ELISA Kit PicoKine®

EK0590

96 wells/kit, with removable strips.

Mouse VEGFR2/KDR ELISA Kit PicoKine®

96 wells/kit, with removable strips.

Mouse VEGFR2/KDR ELISA Kit PicoKine® (96 Tests). Quantitate Mouse Kdr in cell culture supernatants and serum. Sensitivity: 2pg/ml.

Mouse

ELISA

KDR

P35918

Expression system for standard: NS0; Immunogen sequence: A20-E762

There is no detectable cross-reactivity with other relevant proteins.

62.5 pg/ml - 4,000 pg/ml

<2 pg/ml

cell culture supernatants and serum

monoclonal antibody from rat, polyclonal antibody from goat

Store at 4°C for 6 months, at -20°C for 12 months. Avoid multiple freeze-thaw cycles (Ships with gel ice, can store for up to 3 days in room temperature. Freeze upon receiving.)

Vascular endothelial growth factor receptor 2

Vascular endothelial growth factor receptor 2;VEGFR-2;2.7.10.1;Fetal liver kinase 1;FLK-1;Kinase NYK;Protein-tyrosine kinase receptor flk-1;CD309;Kdr;Flk-1, Flk1;

Vascular endothelial growth factor receptor 2

152517 MW

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.

Cell junction . Endoplasmic reticulum . Colocalizes with ERN1 and XBP1 in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (By similarity). Localized with RAP1A at cell-cell junctions.

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.

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.

Vascular endothelial growth factor receptor 2 (VEGFR-2) is a VEGF receptor. This receptor, known as kinase insert domain receptor, is a type III receptor tyrosine kinase. It is mapped to 4q12. This gene encodes one of the two receptors of the VEGF. It functions as the main mediator of VEGF-induced endothelial proliferation, survival, migration, tubular morphogenesis and sprouting. The signalling and trafficking of this receptor are regulated by multiple factors, including Rab GTPase, P2Y purine nucleotide receptor, integrin alphaVbeta3, T-cell protein tyrosine phosphatase, etc. VEGF receptor 2 and the adherens junction act as shear-stress cotransducers, mediating the transduction of shear-stress signals into vascular endothelial cells. In addition to those, VEGFR-2 is also a positive functional marker defining stem cells and distinguishing them from progenitors.

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