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Biotechnol J. 2012 May;7(5):620-34. doi: 10.1002/biot.201100155. Epub 2012 Jan 10.

Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications.

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Department of Chemical Engineering, University of Delaware, Newark, DE, USA.


Protein fusion tags are indispensible tools used to improve recombinant protein expression yields, enable protein purification, and accelerate the characterization of protein structure and function. Solubility-enhancing tags, genetically engineered epitopes, and recombinant endoproteases have resulted in a versatile array of combinatorial elements that facilitate protein detection and purification in microbial hosts. In this comprehensive review, we evaluate the most frequently used solubility-enhancing and affinity tags. Furthermore, we provide summaries of well-characterized purification strategies that have been used to increase product yields and have widespread application in many areas of biotechnology including drug discovery, therapeutics, and pharmacology. This review serves as an excellent literature reference for those working on protein fusion tags.

[Indexed for MEDLINE]

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