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Inhibitor Screening Utilizing Human Kinase Multiplex Arrays
Nathaniel Sahli, David Finkel, Marnie Lindberg, Christpher Buehl, Steve Stoesz, Roberto Campos-Gonzalez and Kathryn Brumbaugh
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis MN, R&D Systems Inc., Minneapolis MN, Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI
Sponsored by R&D Systems, Inc.
Published in July 2011 2011 (p.5) Sponsored,vendor-submitted protocol
Protein kinases regulate many different signaling pathways and cellular processes. They have been implicated in various cancers, typically displaying increased activation, and are now being investigated as potential therapeutic targets. Thus, while investigating potential anti-cancer drugs, it would be beneficial to utilize assay techniques that allow a high-throughput analysis of kinase phosphorylation. The Proteme Profiler ™ 96 Human Phospho-Kinase Array is a microplate-based multiplex immunoassay that employs a two-site sandwich immunoassay technique to simultaneously measure changes in the phosphorylation of multiple intracellular kinases. This assay utilizes a 96-well microplate pre-spotted with a series of antibodies to immobilize different kinases present in a sample. A cocktail of phospho-specific biotinylated detection antibodies and Streptavidin-HRP are subsequently used to detect the bound proteins. A chemiluminescent substrate mix and a camera imaging-system are used to determine the relative amount of analyte bound in individual spots.
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