Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 12, Issue 3, Pages 825-831Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.O112.027094
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Funding
- National Institutes of Health from NCI Clinical Proteomics Tumor Analysis Consortium Initiative [U24CA160034]
- NHLBI [HHSN268201000033C, R01HL096738]
- Broad Institute of Massachusetts Institute of Technology
- Harvard University
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Detection of endogenous ubiquitination sites by mass spectrometry has dramatically improved with the commercialization of anti-di-glycine remnant (K-epsilon-GG) antibodies. Here, we describe a number of improvements to the K-epsilon-GG enrichment workflow, including optimized antibody and peptide input requirements, antibody cross-linking, and improved off-line fractionation prior to enrichment. This refined and practical workflow enables routine identification and quantification of similar to 20,000 distinct endogenous ubiquitination sites in a single SILAC experiment using moderate amounts of protein input. Molecular & Cellular Proteomics 12: 10.1074/mcp.O112.027094, 825-831, 2013.
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