Aarhus University Seal / Aarhus Universitets segl

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

Standard

Affinity proteomics to study endogenous protein complexes : Pointers, pitfalls, preferences and perspectives. / Lacava, John; Molloy, Kelly R.; Taylor, Martin S.; Domanski, Michal; Chait, Brian T.; Rout, Michael P.

In: BioTechniques, Vol. 58, No. 3, 2015, p. 103-119.

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

Harvard

Lacava, J, Molloy, KR, Taylor, MS, Domanski, M, Chait, BT & Rout, MP 2015, 'Affinity proteomics to study endogenous protein complexes: Pointers, pitfalls, preferences and perspectives', BioTechniques, vol. 58, no. 3, pp. 103-119. https://doi.org/10.2144/000114262

APA

Lacava, J., Molloy, K. R., Taylor, M. S., Domanski, M., Chait, B. T., & Rout, M. P. (2015). Affinity proteomics to study endogenous protein complexes: Pointers, pitfalls, preferences and perspectives. BioTechniques, 58(3), 103-119. https://doi.org/10.2144/000114262

CBE

Lacava J, Molloy KR, Taylor MS, Domanski M, Chait BT, Rout MP. 2015. Affinity proteomics to study endogenous protein complexes: Pointers, pitfalls, preferences and perspectives. BioTechniques. 58(3):103-119. https://doi.org/10.2144/000114262

MLA

Vancouver

Lacava J, Molloy KR, Taylor MS, Domanski M, Chait BT, Rout MP. Affinity proteomics to study endogenous protein complexes: Pointers, pitfalls, preferences and perspectives. BioTechniques. 2015;58(3):103-119. https://doi.org/10.2144/000114262

Author

Lacava, John ; Molloy, Kelly R. ; Taylor, Martin S. ; Domanski, Michal ; Chait, Brian T. ; Rout, Michael P. / Affinity proteomics to study endogenous protein complexes : Pointers, pitfalls, preferences and perspectives. In: BioTechniques. 2015 ; Vol. 58, No. 3. pp. 103-119.

Bibtex

@article{77617571bb5e46c282455d3a41c2acaf,
title = "Affinity proteomics to study endogenous protein complexes: Pointers, pitfalls, preferences and perspectives",
abstract = "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.",
keywords = "Affinity, Interactomics, Protein complex, Protein purification, Proteomics",
author = "John Lacava and Molloy, {Kelly R.} and Taylor, {Martin S.} and Michal Domanski and Chait, {Brian T.} and Rout, {Michael P.}",
year = "2015",
doi = "10.2144/000114262",
language = "English",
volume = "58",
pages = "103--119",
journal = "BioTechniques",
issn = "0736-6205",
publisher = "Informa Healthcare",
number = "3",

}

RIS

TY - JOUR

T1 - Affinity proteomics to study endogenous protein complexes

T2 - Pointers, pitfalls, preferences and perspectives

AU - Lacava, John

AU - Molloy, Kelly R.

AU - Taylor, Martin S.

AU - Domanski, Michal

AU - Chait, Brian T.

AU - Rout, Michael P.

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

KW - Affinity

KW - Interactomics

KW - Protein complex

KW - Protein purification

KW - Proteomics

UR - http://www.scopus.com/inward/record.url?scp=84924404035&partnerID=8YFLogxK

U2 - 10.2144/000114262

DO - 10.2144/000114262

M3 - Journal article

C2 - 25757543

AN - SCOPUS:84924404035

VL - 58

SP - 103

EP - 119

JO - BioTechniques

JF - BioTechniques

SN - 0736-6205

IS - 3

ER -