The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
This product is analog to the human VEGF-C156S mutant and only active toward VEGFR-3/FLT -4 but, unlike wild type VEGF-C, is unable to bind to and to activate signalling through VEGFR-2/KDR.
Measured by its ability to stimulate phosphorylation of the VEGFR-3/FLT-4 receptor in porcine aortic endothelial cells (PAE/FLT -4 cells). The ED50 for this effect is typically 150-300 ng/ml. Inactive in the vascular permeability assay.
% SDS-PAGE. Purity >90% by SDS-PAGE and visualised by silver stain.
Product is a point mutant generated by the replacement of the second conserved Cys residue of the recombinant processed VEGFC by a Ser residue.
Source: Insect cells.
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Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Constituents: PBS, BSA
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Reconstitution: The lyophilised VEGFC is soluble in water and most aqueous buffers. The lyophilised VEGFC should be reconstituted in PBS or medium to a concentration not lower than 50 µg/ml.
FLT4 ligand DHM
Vascular endothelial growth factor C
Vascular endothelial growth factor related protein
Vascular endothelial growth factor-related protein
Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-2 (KDR/FLK1) and VEGFR-3 (FLT4) receptors.
Spleen, lymph node, thymus, appendix, bone marrow, heart, placenta, ovary, skeletal muscle, prostate, testis, colon and small intestine and fetal liver, lung and kidney, but not in peripheral blood lymphocyte.
Belongs to the PDGF/VEGF growth factor family.
Undergoes a complex proteolytic maturation which generates a variety of processed secreted forms with increased activity toward VEGFR-3, but only the fully processed form could activate VEGFR-2. VEGF-C first form an antiparallel homodimer linked by disulfide bonds. Before secretion, a cleavage occurs between Arg-227 and Ser-228 producing an heterotetramer. The next extracellular step of the processing removes the N-terminal propeptide. Finally the mature VEGF-C is composed mostly of two VEGF homology domains (VHDs) bound by non-covalent interactions.