Bacterial E. coli Protein Expression

NEB offers two bacterial protein expression systems in E.coli; the NEBExpress® MBP Fusion and Purification System (NEB #E8201) and the IMPACT System (NEB #E6901). Both systems can generate and purify high yields of recombinant proteins.

The NEBExpress® MBP Fusion and Purification System (NEB #E8201) takes advantage of the strong Ptac promoter and the translation initiation signals of maltose binding protein (MBP) to enhance solubility and expression levels of a desired protein in E. coli. The resulting product is an MBP fusion protein, which is then purified by affinity chromatography.

The IMPACT System (NEB #E6901) allows fusion of a tag consisting of an intein and a chitin binding domain (CBD) to either the C-terminus (pTXB1) or the N-terminus (pTYB21) of a target protein. In the presence of thiols, such as DTT, the intein undergoes specific self-cleavage, which releases the target protein from the chitin-bound intein tag resulting in purification of the target protein in a single chromatographic step with no need for proteases.

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Bacterial E. coli Protein Expression includes these subcategories:
NEBExpress MBP Fusion and Purification System
FAQs for Bacterial E. coli Protein Expression
Protocols for Bacterial E. coli Protein Expression
    Publications related to Bacterial E. coli Protein Expression
    • Guan, C.D., Li, P., Riggs, P.D., and Inouye, H. (1988) Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene; 67, 21-30. PubMedID: 2843437
    • Chong, S., Mersha, F.B., Comb, D.G., Scott, M.E., Landry, D., Vence, L.M., Perler, F.B., Benner, J., Kucera, R.B., Hirvonen, C.A., Pelletier, J.J., Paulus, H., and Xu, M.Q. (1997) Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element. Gene; 192, 271-281. PubMedID: 9224900
    • Yu, H. H., et. al. (2010) Expressed protein ligation for the preparation of fusion proteins with cell penetrating peptides for endotoxin removal and intracellular delivery Biochim Biophys Acta; PubMedID: 20170629
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