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A Homogeneous Assay to Quantify Endogenous AKT Phosphorylation in Human Umbilical Endothelial CellsDownload
October 19, 2010
Authors: Brad Larson, Peter Banks, BioTek Instruments, Inc., Winooski, Vermont; Stephanie Nickles, George Klarmann, Lonza, Inc., Walkersville, Maryland; Sylvie Crawford, Bedford, Massachusetts
AKT is a serine/threonine protein kinase that plays a role in key cellular processes. These include the cell cycle, metabolism, and angiogenesis. Activated AKT has been implicated in the proliferation and survival of cells, leading to tumor development. Because of these functions, AKT has become a popular target for drug discovery campaigns, due to the fact that AKT inhibitors may help to treat a number of cancers. Here we demonstrate a homogeneous assay to probe AKT phosphorylation at its serine 473 residue using endogenous levels of kinase expression within human primary HUVEC cells. Validation data demonstrate that the combination of assay and instrument are sensitive enough to detect endogenous phosphorylation of this important drug target.