E. coli has always been the first organism of choice for the researchers for the production of recombinant proteins. It offers rapid and economical production of recombinant proteins and is known to be a well-established expression platform. However, the major problems associated with the E. coli expression system is recovering maximum properly folder proteins. To overcome this, typically some of the fusion tags are used for the expression of proteins. This tags not only helps in increasing the yield of fusion proteins produced. But some of them allow affinity based chromatographic purification. Subsequent removal of these fusion tags using specific proteases.
Aim and Objective: This article gives an overview of the fusion tag technology used for overproduction of recombinant proteins.
Key words: E. coli: Escherichia coli; TRX: Thioredoxin; SUMO: Small Ubiquitin like modifier protein; GST: Glutathione S transferase; CPD: Cysteine Protease Domain; CBD: Chitin Binding Domain