Creating an Efficient Strain for Purity of TEV-Labeled Recombinant Proteins

In this paper we try to describe our experimental and theoretical results. In this study, a new subspecies of Shuffle T۷ Express E. coli was obtained by transformation of an expression plasmid, which could produce the soluble and active TEV protease. This protease could cleave its specific site between TRX and IGF-۱ in the host bacterial cells and separate TRX tag from the recombinant IGF-۱, which was expressed by an independent pET vector. Therefore, by this approach there is no need to digest the recombinant fusion protein after extraction from the bacteria. Indeed, in vivo digestion of recombinant fusion protein can have a significant effect on facilitating and reducing the costs of downstream purification process.