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

Lai Qiang Ying; Bruce P. Branchaud

doi:10.1021/bc200038t

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 journal › Article › peer-review

15 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-EDT² and ReAsH-EDT². An application of the SplAsH tag for affinity purification of tetracysteine-tagged proteins is reported.

Original language	English (US)
Pages (from-to)	987-992
Number of pages	6
Journal	Bioconjugate Chemistry
Volume	22
Issue number	5
DOIs	https://doi.org/10.1021/bc200038t
State	Published - May 18 2011
Externally published	Yes

ASJC Scopus subject areas

Biotechnology
Bioengineering
Biomedical Engineering
Pharmacology
Pharmaceutical Science
Organic Chemistry

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AB - 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-EDT2 and ReAsH-EDT2. An application of the SplAsH tag for affinity purification of tetracysteine-tagged proteins is reported.

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

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