VEGFR3 Extracellular Domain (human, recombinant)

FLT4|Fms-like Tyrosine Kinase 4|Tyrosine-protein Kinase Receptor FLT4|Vascular Endothelial Growth Factor Receptor 3

VEGFR3 is a receptor tyrosine kinase that 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.{60406,60405} It contains an N-terminal signal peptide cleavage site at Tyr25 and can also be cleaved between Arg472 and Ser473 creating an alternate N-terminus.{61388,61389} VEGFR3 forms homodimers or heterodimers with VEGFR2, with heterodimerization inducing changes in VEGFR3 autophosphorylation patterns.{60405} It is expressed in lymphatic endothelial cells, where it is bound by the growth factors VEGF-C or VEGF-D and involved in cell proliferation, migration, and survival, as well as in cells undergoing angiogenesis or lymphangiogenesis, and in osteoblasts, neuronal progenitor cells, and macrophages.{60405,60406} Inactivating mutations in VEGFR3 have been found in patients with hereditary lymphedema.{60410,60411} Activation of VEGFR3 signaling increases tumor growth in a mouse orthotopic model of colorectal cancer, and VEGFR3 protein levels are increased in tumor tissue and tumor-associated macrophages isolated from patients with non-metastatic colorectal cancer.{60412} Cayman's VEGFR3 Extracellular Domain (human, recombinant) protein can be used for enzyme activity assays. This protein consists of 763 amino acids, has a calculated molecular weight of 86 kDa, and a predicted N-terminus of Tyr25 after signal peptide cleavage. By SDS-PAGE, under non-reducing conditions, the apparent molecular mass of the protein is approximately 130 kDa due to glycosylation.

-80

-80

Lyophilized from sterile PBS, pH 7.4

365

≥97% estimated by SDS-PAGE