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Protein Expression

Recombinant production of proteins is one of the most powerful techniques used in the Life Sciences. The ability to produce and purify an abundance of a desired recombinant protein can permit a wide range of possibilities including its use in industrial processes, or its use to diagnose or treat disease.

At first glance, recombinant protein expression may appear simple. Essentially, DNA encoding a target protein is cloned downstream of a promoter in an expression vector. This vector is then introduced into a host cell, and the cell’s protein synthesis machinery produces the desired protein. In practice, however, protein expression can be very challenging because so many factors may influence the process. For example, each protein folds in its own unique manner, a process that may be influenced by the choice of expression host. Similarly, some proteins require post-translational modifications or proper insertion into a biological membrane. Finally, some proteins may have an activity that is detrimental to the host. Thus, no single solution exists for successful production of all recombinant proteins. Instead, it is beneficial to have access to a wide range of expression tools, and a willingness to explore multiple approaches to better one’s chances for success. Protein Expression at NEB.

 

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Protein Expression includes these areas of focus:
Cell-Free Protein Expression
NEBExpress® Cell-free E. coli Protein Synthesis System
PURExpress
Protein Expression in Yeast
Expression of Difficult Proteins
Disulfide-bonded Protein Expression
Membrane Protein Expression
Toxic Protein Expression
Target Protein Insolubility
Protein Expression in E. Coli
T7 Expression
Non-T7 Expression
FAQs for Protein Expression
Protocols for Protein Expression
Application Notes for Protein Expression
    Publications related to Protein Expression
  1. Agrawal, A., Bisharyan, Y., Papoyan, A, Bednenko, J., Cardarelli, J., Yao, M., Clark, T., Berkm​en, 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 Expr Purif. 153, PubMedID: 30081196, DOI: 10.1016/j.pep.2018.08.001.
  2. 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 J Biol Chem. 294(48), PubMedID: 31604819, DOI: 10.1074/jbc.RA119.011008
  3. Manta, Bruno; Berkmen, Mehmet; 2019. Disulfide Bond Formation in the Periplasm of <em>Escherichia coli.</em> EcoSal Plus. , PubMedID: 30761987, DOI: 10.1128/ecosalplus.ESP-0012-2018.
  4. Sakhtah, H., Behler, J., Ali-Reynolds, A., Causey, T.B., Vainauskas, S., Taron, C.H. 2019. A novel regulated hybrid promoter that permits autoinduction of heterologous protein expression in <em>Kluyveromyces lactos</em> Appl Environ Microbiol. , PubMedID: 31053583, DOI:
  5. Reuter, W.H., Masuch, T., Ke, N., Lenon, M., Radzinski, M., Van Loi, V., Ren, G., Riggs, P., Antelmann, H., Reichmann, D., Leichert, L.I., Berkmen, M 2019. Utilizing redox-sensitive GFP fusions to detect <em>in vivo</em> redox changes in a genetically engineered prokaryote Redox Biol. 26, PubMedID: 31450103, DOI: 10.1016/j.redox.2019.101280
  6. 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
  7. Chuzel, L., Ganatra, M.B., Schermerhorn, K.M., Gardner, A.F., Anton, B.P., Taron, C.H. 2017. Complete genome sequence of Kluyveromyces lactis strain GG799, a common yeast host for heterologous protein expression Genome Announc. 5(30), PubMedID: 28751387, DOI:
  8. Ke, Na; Berkmen, Mehmet; Ren, Guoping; 2017. A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo Nat Chem Biol. 13, PubMedID: 28628094, DOI: 10.1038/nchembio.2409
  9. 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.
  10. Anton, B.P., Fomenkov, A., Raleigh, E.A. and Berkmen, M. 2016. Complete Genome Sequence of the Engineered Escherichia coli SHuffle Strains and Their Wild-Type Parents Genome Announc. Mar 31;4(2), PubMedID: 27034504, DOI: 10.1128/genomeA.00230-16.
  11. Chatelle C, Kraemer S, Ren G, Chmura H, Marechal N, Boyd D, Roggemans C, Ke N, Riggs P, Bardwell J, Berkmen M 2015. Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase Antioxid Redox Signal. , PubMedID: 26191605, DOI: 10.1089/ars.2014.6235
  12. 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 Nat Commun. (6)8072, PubMedID: 26311203, DOI: 10.1038/ncomms9072.
  13. Berkmen, M. 2012. Production of disulfide-bonded proteins in Escherichia coli Protein Expr Purif. , PubMedID: 22085722, DOI:
  14. 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
  15. 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:
  16. Mauris, J.and Evans, T.C., Jr. 2010. A human PMS2 homologue from Aquifex aeolicus stimulates an ATP-dependent DNA helicase. J Biol Chem. 285(15), PubMedID: 20129926, DOI:
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