Affinity proteomics to study endogenous protein complexes: Pointers, pitfalls, preferences and perspectivesLaCava, J., Molloy, K. R., Taylor, M. S., Domanski, M., Chait, B. T. & Rout, M. P., Mar-2015, In : Biotechniques. 58, 3, p. 103-119 14 p.
Research output: Contribution to journal › Review article › Academic › peer-review
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.
|Number of pages||14|
|Publication status||Published - Mar-2015|
- protein complex, protein purification, affinity, proteomics, interactomics, NUCLEAR-PORE COMPLEX, PURIFICATION-MASS-SPECTROMETRY, INDUCIBLE GENE-EXPRESSION, EPSTEIN-BARR-VIRUS, MAMMALIAN-CELLS, SACCHAROMYCES-CEREVISIAE, MOLECULAR ARCHITECTURE, BAC TRANSGENEOMICS, ENHANCED DETECTION, RAPID PRODUCTION