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

Angela M. Martin, Ting Liu, Bert C. Lynn, Anthony P. Sinai

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

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.

Original languageEnglish
Pages (from-to)4758-4762
Number of pages5
JournalJournal of Proteome Research
Volume6
Issue number12
DOIs
StatePublished - Dec 2007

Keywords

  • Biotin
  • Immunoprecipitation
  • Mass spectrometry
  • Streptavidin
  • Toxoplasma

ASJC Scopus subject areas

  • General Chemistry
  • Biochemistry

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