Harnessing Affinity Tags for Recombinant Protein Purification: Concepts, Methods, and Troubleshooting

Efficient purification of recombinant proteins is essential for both fundamental biochemical research as well as industrial biotechnology applications. The use of affinity tags has emerged as one of the most powerful and widely adopted method for protein purification. This paper contains recent advancements of design and functions of different affinity tags namely, polyhistidine (His-tag), glutathione S-transferase (GST), small ubiquitin-like modifier (SUMO) tag, maltose-binding protein (MBP), calmodulin-binding protein (CBP), intein-chitin-binding domain tag, N-utilization substance A tag, Halo Tag®, PDZ domain-based tags, thioredoxin tag, polyarginine (Arg-tag) and polyaspartate (Asp-tag) tags, and heparin-binding tag used in recombinant protein purification in bacteria. In addition, we discuss the merits and demerits of each affinity tag.