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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.