| Scientific Poster
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Orbitrap Exploris 480
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SureQuant Quantitation
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Toward a Single Comprehensive Assay for Protein Expression of the Human Kinome
Robert Sprung1, Aaron Gajadhar2a, Michael East3, Petra Gilmore1, Daniel Lopez Ferrer2a, Bhavin Patel2b, Sebastien Gallien2c, Dennis Goldfarb1, Ben Major1, Gary L. Johnson3, R. Reid Townsend1
International Hupo 2020 1Washington University School of Medicine, St. Louis, MO 63110
2aThermo Fisher Scientific, San Jose, CA; 2bRockford, IL; 2cParis, France.
3University of North Carolina School of Medicine, Chapel Hill, NC 27599
The human kinome is comprised of 518 protein and lipid kinases which play a fundamental role in the propagation and integration of cell signaling events. Dysregulation of kinase expression and activity plays a critical role in human disease with >55 kinase inhibitors in the clinic or late-stage trials. Inhibitor resistance develops, in part, due to an adaptive response involving multiple classes of kinases. Yet, comprehensive quantification of cellular kinase levels remains challenging. We report a single LC-MS assay that reproducibly quantifies 976 stable isotope labeled peptides for 367 kinases in a single LC-MS analysis using a new internal standard-triggered acquisition method.
The human kinome is comprised of 518 protein and lipid kinases which play a fundamental role in the propagation and integration of cell signaling events. Dysregulation of kinase expression and activity plays a critical role in human disease with >55 kinase inhibitors in the clinic or…
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