title: New trends and affinity tag designs for recombinant protein purification.
abstract: Engineered purification tags can facilitate very efficient 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 more recently, compound multifunctional tags with optimized capabilities. Although classic proteases are still primarily used to remove the tags from target proteins, new self-cleaving methods are gaining traction as a highly convenient alternative. In this review, we discuss some of these emerging trends, and examine their potential impacts and remaining challenges in recombinant protein research.
authors.affiliation: Department of Chemical & Biomolecular Engineering, 435 Koffolt Laboratories, 140 W Nineteenth Avenue, Columbus, OH 43210, United States. Electronic address: wood.750@osu.edu.
authors.forename: David W
authors.initials: DW
authors.lastname: Wood
mesh_terms: D000345:Affinity Labels / Q000737:chemistry*; D015195:Drug Design; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry* / Q000302:isolation & purification*
chemical_list: D000345:Affinity Labels; D064267:Intrinsically Disordered Proteins; D011994:Recombinant Proteins