Purification of tetracysteine-tagged proteins by affinity. Chromatography using a non-fluorescent, photochemically stable bisarsenical affinity ligand

Lai Qiang Ying, Bruce P. Branchaud

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

The use of genetically encoded small peptide tags such as polyhistidine and tetracysteine tags has become important for protein purification and enrichment. An improved affinity purification of tetracysteine (CCXXCC) tagged proteins has been achieved using a nonfluorescent, photochemically stable bisarsenical affinity ligand SplAsH. The photochemical stability of the SplAsHbiotin, shown in compound 5, is superior to FlAsH-EDT 2 and ReAsH-EDT 2. An application of the SplAsH tag for affinity purification of tetracysteine-tagged proteins is reported.

Original languageEnglish (US)
Pages (from-to)987-992
Number of pages6
JournalBioconjugate Chemistry
Volume22
Issue number5
DOIs
StatePublished - May 18 2011

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomedical Engineering
  • Pharmacology
  • Pharmaceutical Science
  • Organic Chemistry

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