Simple and effective affinity purification procedures for mass spectrometry-based identification of protein-protein interactions in cell signaling pathways

Julian H.M. Kwan, Andrew Emili

Research output: Chapter in Book/Report/Conference proceedingChapter

3 Scopus citations

Abstract

Identification of protein-protein interactions can be a critical step in understanding the function and regulation of a particular protein and for exploring intracellular signaling cascades. Affinity purification coupled to mass spectrometry (APMS) is a powerful method for isolating and characterizing protein complexes. This approach involves the tagging and subsequent enrichment of a protein of interest along with any stably associated proteins that bind to it, followed by the identification of the interacting proteins using mass spectrometry. The protocol described here offers a quick and simple method for routine sample preparation for APMS analysis of suitably tagged human cell lines.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages181-187
Number of pages7
DOIs
StatePublished - Jan 1 2016
Externally publishedYes

Publication series

NameMethods in Molecular Biology
Volume1394
ISSN (Print)1064-3745

Keywords

  • Affinity purification-mass spectrometry
  • Cell signaling pathway
  • Liquid chromatography-mass spectrometry

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Fingerprint

Dive into the research topics of 'Simple and effective affinity purification procedures for mass spectrometry-based identification of protein-protein interactions in cell signaling pathways'. Together they form a unique fingerprint.

Cite this