Purification of specific chromatin loci for proteomic analysis

Stephanie D. Byrum, Sean D. Taverna, Alan J. Tackett

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Purification of small, native chromatin regions for proteomic identification of specifically bound proteins and histone posttranslational modifications is a powerful approach for studying mechanisms of chromosome metabolism. Here we detail a C hromatin A ffinity P urification with M ass S pectrometry (ChAP-MS) approach for affinity purification of 1 kb regions of chromatin for targeted proteomic analysis. This approach utilizes quantitative, high resolution mass spectrometry to categorize proteins and histone posttranslational modifications co-enriched with the given chromatin region as either “specific” to the targeted chromatin or “nonspecific” contamination. In this way, the ChAP-MS approach can help define and redefine mechanisms of chromatin-templated activities.

Original languageEnglish (US)
Pages (from-to)83-92
Number of pages10
JournalMethods in Molecular Biology
StatePublished - 2015


  • Chromatin
  • Epigenetics
  • Histone
  • Posttranslational modification
  • Proteomics
  • Purification

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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