Research progress of the affinity tag in the field of recombinant protein purification

Abstract

Engineered purification tags can very efficiently facilitate the purification of recombinant proteins, resulting in high yields and purities in a few standard steps. Over the years, many different purification tags have been developed, including short peptides, epitopes, folded protein domains, non-chromatographic tags and recently developed compound multifunctional tags with optimized capabilities. Although classic proteases are still used as a primary method to remove the tags from the target proteins, new self-cleaving methods are gaining more attention as a highly convenient alternative. In this review, we discuss some of these emerging trends, and examine their potential impacts and novel challenges on recombinant protein research. Key words: Affinity tag; Recombinant protein; Compound multifunctional tags; His tag