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Affinity proteomics to study endogenous protein complexes: Pointers, pitfalls, preferences and perspectives

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • John Lacava, New York University School of Medicine
  • ,
  • Kelly R. Molloy, The Rockefeller University
  • ,
  • Martin S. Taylor, The Sidney Kimmel Comprehensive Cancer Center, The Johns Hopkins University School of Medicine, Baltimore
  • ,
  • Michal Domanski, Laboratory of Cellular and Structural Biology, The Rockefeller University, New York
  • ,
  • Brian T. Chait, The Rockefeller University
  • ,
  • Michael P. Rout, The Rockefeller University

Dissecting and studying cellular systems requires the ability to specifically isolate distinct proteins along with the co-assembled constituents of their associated complexes. Affinity capture techniques leverage high affinity, high specificity reagents to target and capture proteins of interest along with specifically associated proteins from cell extracts. Affinity capture coupled to mass spectrometry (MS)-based proteomic analyses has enabled the isolation and characterization of a wide range of endogenous protein complexes. Here, we outline effective procedures for the affinity capture of protein complexes, highlighting best practices and common pitfalls.

Original languageEnglish
JournalBioTechniques
Volume58
Issue3
Pages (from-to)103-119
Number of pages17
ISSN0736-6205
DOIs
Publication statusPublished - 2015

    Research areas

  • Affinity, Interactomics, Protein complex, Protein purification, Proteomics

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