Send to

Choose Destination
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

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


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.

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for American Chemical Society
Loading ...
Support Center