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  • Discovery of High-Affinity PDGF-VEGFR Interactions: Redefining RTK Dynamics.

Discovery of High-Affinity PDGF-VEGFR Interactions: Redefining RTK Dynamics.

Scientific reports (2017-11-29)
Spencer B Mamer, Si Chen, Jared C Weddell, Alexandra Palasz, Ashley Wittenkeller, Manu Kumar, P I Imoukhuede
ABSTRACT

Nearly all studies of angiogenesis have focused on uni-family ligand-receptor binding, e.g., VEGFs bind to VEGF receptors, PDGFs bind to PDGF receptors, etc. The discovery of VEGF-PDGFRs binding challenges this paradigm and calls for investigation of other ligand-receptor binding possibilities. We utilized surface plasmon resonance to identify and measure PDGF-to-VEGFR binding rates, establishing cut-offs for binding and non-binding interactions. We quantified the kinetics of the recent VEGF-A:PDGFRβ interaction for the first time with K

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Product Description

Sigma-Aldrich
Angiopoietin-4 human, recombinant, expressed in NSO cells, ≥85% (SDS-PAGE), lyophilized powder