Purification of TAP-tagged proteins by two-step pull down from DT40 cells.

Hiroyuki Kitao, Minoru Takata

研究成果: Contribution to journalArticle査読

3 被引用数 (Scopus)

抄録

For proteomic analysis, protein purification from cell extracts is an important step. Since production of high quality antibody is time consuming and not guaranteed to be successful, expression of epitope-tag conjugated protein of interest followed by immunoprecipitation using anti-epitope-tag antibody is a common method for protein purification. Here we describe use of an epitope-tag called TAP (tandem affinity purification) in DT40, which consists of Protein A IgG-binding motif and calmodulin binding motif separated by TEV cleavage site. Tandem purification using two different epitopes should eliminate non-specific binding and help identifying physiological protein-protein associations.

本文言語英語
ページ(範囲)409-413
ページ数5
ジャーナルSub-cellular biochemistry
40
出版ステータス出版済み - 1 1 2006
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学
  • 癌研究

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