pTrham-6XHis-MBP Expression Vector for Improved Protein Solubility

E. coli maltose-binding protein (MBP) enhances the solubility and promotes the proper folding of its fusion partners. Amid Biosciences has engineered and successfully tested pTrham-6XHis-MBP vector based on the rhamnose-inducible pTrham series of expression vectors for the production of dual His-MBP-tagged fusion proteins in the cytoplasm of E. coli. The MBP moiety improves the yield and solubility of its fusion partners while the His-tag facilitates and simplifies their purification with Immobilized Metal Ion Affinity Chromatography (IMAC) resins. Furthermore, the MBP tag allows for affinity purification of the fusion product on the amylose resin. pTrham-6xHis-MBP vector encodes an N-terminal 6xHis-MBP tag followed by a TEV (Tobacco Etch Virus) protease cleavage site. The TEV site enables removal of the MBP tag from the protein following production. TEV is reported to have better specificity for its recognition site compared to EKT Thrombin or Factor Xa proteases. pTrham-6xHis-MBP has