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.
- Protein Expression in E. Coli
- T7 Expression
- Non-T7 Expression
- Cell-Free Protein Expression
- NEBExpress® Cell-free E. coli Protein Synthesis System
- Protein Expression in Yeast
- Expression of Difficult Proteins
- Disulfide-bonded Protein Expression
- Membrane Protein Expression
- Toxic Protein Expression
- Target Protein Insolubility
- Protein Expression Using BL21(DE3) (C2527)
- Protein Expression with T7 Express strains
- Expression Using SHuffle®
- Protein Synthesis Reaction using PURExpress (E6800)
- Western Analysis (E8023)
- Transformation Protocol (C2530)
- Protocol for Protein Expression Using BL21 (C2530)
- 5 Minute Transformation Protocol (C2530)
- Expression Using SHuffle (C3027)
- Use SNAP-Capture Pull Down Resin (S9144)
- Electroporation Protocol (C2986)
- Expression Using SHuffle (C3026)
- E. coli Lemo21(DE3)
- Co-expression of Multiple Proteins in Kluyveromyces lactis
- Protein Expression with T7 Express Strains
- Transformation of SHuffle® Competent Cell Strains
- Use of the PURExpress® in vitro Protein Synthesis Kit, Disulfide Bond Enhancer and SHuffle® Competent E. coli for heterologous in vitro and in vivo cellulase expression.
- Using the PURExpress® In Vitro Protein Synthesis Kit for Heterologous In Vitro Expression and Functional Screening of FMN-dependent Oxidoreductase Variants
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.
The Future of Cell-Free Protein Synthesis
Cell-free protein synthesis has the potential to become one of the most important high throughput technologies for functional genomics and proteomics.
The Next Generation of Reagents for Sample Preparation
Why Choose the K. lactis Protein Expression Kit?
Review the advantages of the K. lactis Protein Expression Kit for rapid, high yield protein expression in yeast.
Avoid Common Obstacles in Protein Expression
Read how to avoid common obstacles in protein expression that prevent interactions with cellular machinery.
- Competent Cell Brochure
- Protein Expression & Purification Brochure
- DNA Sequences and Maps Tool
- Competent Cell Product Comparison
- IMPACT™ Vectors and Applications
- Protein Expression and Purification Selection Chart
- Convenient Formats of Competent Cells
- An E.coli lysate-based system for in vitro Protein Synthesis
- 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 Kluyveromyces lactos Appl. Environ. Microbiol.. , PubMedID: 31053583, DOI:
- 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 Announcements. 5(30), PubMedID: 28751387, DOI:
- 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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NEB has a long history in recombinant protein expression and has developed a wide array of solutions for proteins that are difficult to express.