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Updated: Jun 2, 2026

Affinity Purification of a 6X-His-Tagged Protein using a Fast Protein Liquid Chromatography System
Published on: April 26, 2024
Purification of tetracysteine-tagged proteins by affinity chromatography using a non-fluorescent, photochemically
Lai-Qiang Ying1, Bruce P Branchaud
1Life Technologies, 29851 Willow Creek Road, Eugene, OR 97402, United States. lai-qiang.ying@lifetech.com
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 SplAsH-biotin, 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.
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