Biochem/physiol Actions
Measured by the ability to inhibit VEGF165-induced proliferation in human umbilical vein endothelial (HUVE) cells
General description
Recombinant, human VEGFR-2 consisting of all 7 immunoglobulin-like extracellular domains, but lacking the single transmembrane region and the intracellular split tyrosine kinase domain expressed in S. frugiperda insect cells. Binding of ligand to the full-length VEGFR-2 results in a high signaling activity and mitogenic activity in endothelial cells.
Recombinant, human VEGFR-2 consisting of all 7 immunoglobulin-like extracellular domains, but lacking the single transmembrane region and the intracellular split tyrosine kinase domain expressed in S. frugiperda insect cells. Contains all of the domains necessary for high affinity binding to VEGF. VEGFR-2 has a lower affinity for VEGF165 than VEGFR-1. However, VEGFR-2 has a higher signaling activity and is reported to mediate almost all observed endothelial cell responses to VEGF, including the increased microvascular permeability and endothelial cell proliferation. VEGFR-2 requires heparin for binding VEGF165.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Other Notes
Robinson, C.J., and Stringer, S.E. 2001 J. Cell Sci.114, 853.Roeckl, W., et al. 1998. Exp. Cell Res.241, 161.
Packaging
50 µg in Plastic ampoule
Physical form
Lyophilized from 100 mM NaCl, 25 mM MES, pH 5.5.
Reconstitution
Following reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 6 months at -70°C. Avoid freeze/thaw cycles of solutions.
Warning
Toxicity: Standard Handling (A)
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