VEGF-A (also called VEGF) and its receptors represent the best characterized signalling pathway in developmental and tumour angiogenesis. VEGF-A binds to two receptor-tyrosine kinases: VEGFR-1/Flt-1 and VEGFR-2/KDR. VEGFR-2 is the major mediator of the mitogenic, angiogenic and permeability-enhancing effects of VEGF-A. The VEGFR's possess an approximately 750 amino acid residue extracellular domain, which is organized into seven immunoglobulin (Ig)- like folds. This extracellular domain is followed by a single transmembrane region, a juxtamembrane domain, a split tyrosine-kinase domain interrupted by a 70-amino acid kinase insert and a C-terminal tail. Alternative splicing or proteolytic processing of VEGFR's give rise to secreted variants of VEGFR-2, also called soluble VEGFR-2. Although the VEGFR's are primarily expressed in the vascular system, sensitive methods like sandwich ELISA's have allowed the detection of VEGFR expression in non-endothelial cells like hematopoietic stem cells. Besides its putative role as a surrogate marker for tumour angiogenesis, naturally occurring sVEGFR-2 is a molecular regulator for VEGF and VEGFR signalling. Sample Types: Human cell culture, citrate plasma, EDTA plasma, heparin plasma, serum. Sample Size: 50 μL. Range: 78 - 5,000 pg/mL. Sensitivity: 7.0 pg/mL. Time: 3hr 30min
Size
96 wells
Concentration
n/a
Applications
Immunoassays. Research Use Only. Not for Use in Diagnostic Procedures.