Robert Clifford, Susanna Lindman, Jie Zhu, Ethan Luo, Jared Delmar, Yeqing Tao, Kuishu Ren, Abigail Lara, Corinne Cayatte, Patrick McTamney, Ellen O'Connor, Johan Öhman
Affinity tags are frequently engineered into recombinant proteins to facilitate purification. Although this technique is powerful, removal of the tag is desired because the tag can interfere with biological activity and can potentially increase the immunogenicity of therapeutic proteins. Tag removal is complex, as it requires adding expensive protease enzymes. To overcome this limitation, split intein based affinity purification systems have been developed in which a CC -intein tag is engineered into a protein of interest for binding to a NC -intein peptide ligand fixed to a chromatographic support...
April 12, 2024: Journal of Chromatography. A