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Tagging Recombinant Proteins to Enhance Solubility and Aid Purification

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Protein Chromatography

Part of the book series: Methods in Molecular Biology ((MIMB,volume 681))

Abstract

Protein fusion technology has enormously facilitated the efficient production and purification of individual recombinant proteins. The use of genetically engineered affinity and solubility-enhancing polypeptide “tags” has increased greatly in recent years and there now exists a considerable repertoire of these that can be used to solve 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 therefore become indispensable tools for structural and functional proteomic initiatives that involve the expression of many proteins in parallel. Here, the rationale and applications of a range of established and more recently developed solubility-enhancing and affinity tags are outlined.

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Acknowledgments

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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  1. School of Biotechnology and National Centre for Sensor Research, Dublin City University, Dublin, Ireland

    Dermot Walls & Sinéad T. Loughran

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  1. Dermot Walls
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Correspondence to Dermot Walls .

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  1. National Centre for Sensor Research, School of Biotechnology, Dublin City University, Dublin, 9, Ireland

    Dermot Walls

  2. National Centre for Sensor Research, School of Biotechnology, Dublin City University, Dublin, 9, Ireland

    Sinéad T. Loughran

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Walls, D., Loughran, S.T. (2011). Tagging Recombinant Proteins to Enhance Solubility and Aid Purification. In: Walls, D., Loughran, S. (eds) Protein Chromatography. Methods in Molecular Biology, vol 681. Humana Press. https://doi.org/10.1007/978-1-60761-913-0_9

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