A method for quantitative, proteome-wide analysis of protein phosphorylation
Introduction Protein phosphorylation is one of the most important regulatory events in cells. The state of activity of numerous enzymes and processes and the association of specific proteins into functional complexes are frequently controlled by reversible protein phosphorylation. Because cellular proteins are coordinately phosphorylated to control specific biological processes, the complex mechanisms that control biological systems by protein phosphorylation are difficult to investigate using current technology. An MS-based method that allows both the identification of the sites of phosphorylation from complex mixtures of proteins and their quantitation will be an essential part of proteome analysis. Thus, there is a substantial need for a more rapid and general method for the analysis of protein phosphorylation in complex protein mixtures that does not require purification to homogeneity of individual phosphoproteins. Technology description Researchers at the University of Washington have invented a method for selective chemical labeling of phosphate groups which facilitates highly specific purification of molecules containing one or several phosphate group(s). The method is specifically applicable to biological oligomers and polymers, including phosphopeptides, phosphoproteins and phospholipids. When combined with mass spectrometric techniques, the method can be employed to detect and identify phosphorylated proteins in complex mixtures and to precisely identify the phosphorylated amino acid. Business opportunity The invention has application in the field of proteomics where it facilitates the quantitative, global analysis of protein phosphorylation in a cell or tissue. The worldwide proteomics market is expected to reach $17.5 billion by 2009 Intellectual Property Position US 7,052,915: Selective Labeling and Isolation of Phosphopeptides and Applications to Proteome Analysis. Issued May, 2006.
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