Abstract
Protein fusion technology has had a major impact on the efficient production and purification of individual recombinant proteins. The use of genetically engineered affinity and solubility-enhancing polypeptide “tags” has a long history, and there is a considerable repertoire of these that can be used to address issues related to the expression, stability, solubility, folding, and purification of their fusion partner. In the case of large-scale proteomic studies, the development of purification procedures tailored to individual proteins is not practicable, and affinity tags have become indispensable tools for structural and functional proteomic initiatives that involve the expression of many proteins in parallel. In this chapter, the rationale and applications of a range of established and more recently developed solubility-enhancing and affinity tags is described.
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We gratefully acknowledge funding from the Health Research Board (HRB grant RP/2005/212) and Enterprise Ireland (EI grant IP 2008-0530).
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Loughran, S.T., Walls, D. (2023). Tagging Recombinant Proteins to Enhance Solubility and Aid Purification. In: Loughran, S.T., Milne, J.J. (eds) Protein Chromatography. Methods in Molecular Biology, vol 2699. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-3362-5_7
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DOI: https://doi.org/10.1007/978-1-0716-3362-5_7
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