Within the realm of E. coli expression, the T7 system is the most popular approach for producing proteins. In this system, an expression vector containing a gene of interest cloned downstream of the T7 promoter is introduced into a T7 expression host. T7 expression hosts such as DE3 strains or T7 Express strains carry a chromosomal copy of the phage T7 RNA polymerase gene. When inducer is added, T7 RNA polymerase is expressed and becomes dedicated to transcription of the gene of interest.
- 5 Minute Transformation (C2523)
- 5 Minute Transformation Protocol (C2527)
- 5 Minute Transformation Protocol (C2528)
- 5 Minute Transformation Protocol (C2529)
- 5 Minute Transformation Protocol (C2530)
- 5 Minute Transformation Protocol (C2566)
- 5 Minute Transformation Protocol (C3010)
- 5 Minute Transformation Protocol (C3013)
- 5 Minute Transformation Protocol (C3026)
- 5 Minute Transformation Protocol (C3028)
- 5 Minute Transformation Protocol (C3029)
- 5 Minute Transformation Protocol (C3030)
- 5 Minute Transformation Protocol (C3037)
- Expression Using SHuffle (C3026)
- Expression Using SHuffle (C3028)
- Expression Using SHuffle (C3029)
- Expression Using SHuffle (C3030)
- Expression Using NEB Express (C2523)
- Protocol for Expression Using NEB Express Iq (C3037)
- Protocol for Expression Using T7 Express (C2566)
- Protocol for Expression Using T7 Express lysY (C3010)
- Protocol for Expression Using T7 Express lysY/Iq (C3013)
- Protocol for Protein Expression Using BL21 (C2530)
- Protein Expression with T7 Express strains
- Protein Expression Using Lemo21(DE3) (C2528)
- Protein Expression Using BL21(DE3) (C2527)
- Protein Expression Using NiCo21(DE3) (C2529)
Over 40 years in protein expression and purification – a historical perspective
This article provides an overview of the advances in protein expression and purification methodology over the past 40 years.
- Agrawal, A., Bisharyan, Y., Papoyan, A, Bednenko, J., Cardarelli, J., Yao, M., Clark, T., Berkmen, M., Ke, N., Colussi, P. 2019. Fusion to Tetrahymena thermophila granule lattice protein 1 confers solubility to sexual stage malaria antigens in Escherichia coli. Protein Expression and Purification. 153, PubMedID: 30081196, DOI: 10.1016/j.pep.2018.08.001.
- Leith, E.M., O'Dell, W.B., Ke, N., McClung, C., Berkmen, M., Bergonzo, C., Brinson, R.G., Kelman, Z 2019. Characterization of the internal translation initiation region in monoclonal antibodies expressed in Escherichia coli Journal of Biological Chemistry. 294(48), PubMedID: 31604819, DOI: 10.1074/jbc.RA119.011008
- Reddy, P.T., Brinson, R.G., Hoopes, J.T., McClung, C., Ke, N., Kashi, L. 2018. Platform development for expression and purification of stable isotope labeled monoclonal antibodies in Escherichia coli. mAbs Mabs. 10 (7), PubMedID: 30060704, DOI: 10.1080/19420862.2018.1496879
- Ke, Na; Berkmen, Mehmet; Ren, Guoping; 2017. A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo Nature Chemical Biology. 13, PubMedID: 28628094, DOI: 10.1038/nchembio.2409
- Ren, G., Ke, N. and Berkmen, M. 2016. Use of the Shuffle Strains in Production of Proteins. Curr Protoc Protein Sci.. Aug 1, PubMedID: 27479507 , DOI: 10.1002/cpps.11.
- Robinson, M.-P., Ke, N., Lobstein, J., Peterson, C., Szkodny, A., Mansell, T.J., Tuckey, C., Riggs, P.D., Colussi, P.A., Noren, C.J., Taron, C.H., Delisa, M.P., Berkmen, M. 2015. Efficient expression of full-length antibodies in the cytoplasm of engineered bacteria Nature Communications . (6)8072, PubMedID: , DOI: 10.1038/ncomms9072.
- Hemmis, C.W., Berkmen, M., Eser, M.and Schildbach, J.F. 2011. TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance. J Bacteriol. 193(18), PubMedID: 21742866, DOI: 10.1128/JB.00351-11
- Shouldice, S.R., Cho, S.H., Boyd, D., Heras, B., Eser, M., Beckwith, J., Riggs, P., Martin, J.L.and Berkmen, M. 2010. In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling. Mol.Microbiol.. 75(1), PubMedID: 19968787, DOI:
- Manta, Bruno; Berkmen, Mehmet; . Disulfide Bond Formation in the Periplasm of Escherichia coli EcoSal Plus. , PubMedID: , DOI: 10.1128/ecosalplus.ESP-0012-2018.
E. coli Hosts
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NEB has a long history in recombinant protein expression and has developed a wide array of solutions for proteins that are difficult to express.