title: Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications.
abstract: 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.
authors.affiliation: Department of Chemical Engineering, University of Delaware, Newark, DE, USA.
authors.forename: Carissa L
authors.initials: CL
authors.lastname: Young
authors.forename: Zachary T
authors.initials: ZT
authors.lastname: Britton
authors.forename: Anne S
authors.initials: AS
authors.lastname: Robinson
mesh_terms: D000818:Animals; D001709:Biotechnology / Q000379:methods*; D002846:Chromatography, Affinity / Q000379:methods*; D006801:Humans; D010447:Peptide Hydrolases / Q000737:chemistry / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification*; D012995:Solubility
chemical_list: D011993:Recombinant Fusion Proteins; D010447:Peptide Hydrolases