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J Proteome Res. 2007 Dec;6(12):4758-62. Epub 2007 Nov 10.

Elimination of affinity reagent interference for the mass spectrometric detection of low-abundance proteins following immunoprecipitation.

Author information

1
Department of Microbiology, Immunology, and Molecular Genetics and Department of Chemistry, University of Kentucky, Lexington, Kentucky 40536, USA.

Abstract

The presence of affinity reagents such as immunoglobulin in preparations for sensitive mass spectrometry analyses can preclude the identification of low-abundance proteins of interest. We report a method whereby antisera are purified and biotinylated prior to use in immunoprecipitation that allows for its efficient removal from proteomic samples via streptavidin capture. This method can similarly be extended to other affinity reagents such as recombinant fusion proteins for enhanced identification of interacting proteins.

PMID:
17994686
DOI:
10.1021/pr070517a
[Indexed for MEDLINE]

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