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

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 alo...

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Veröffentlicht in:BioTechniques. - 1988. - 58(2015), 3 vom: 13. März, Seite 103-19
1. Verfasser: LaCava, John (VerfasserIn)
Weitere Verfasser: Molloy, Kelly R, Taylor, Martin S, Domanski, Michal, Chait, Brian T, Rout, Michael P
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2015
Zugriff auf das übergeordnete Werk:BioTechniques
Schlagworte:Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't affinity interactomics protein complex protein purification proteomics Multiprotein Complexes Proteins
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520 |a 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 
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