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 looks quite 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.
- Affinity Purification
- Coupled Protein Expression & Purification
- IMPACT™ Protein Expression
- Maltose Binding Protein Expression
- His-tagged Protein Expression
- Yeast Chitin Binding Domain Tag
- Expression of Difficult Proteins
- Disulfide-Bonded Protein Expression
- Membrane Protein Expression
- Toxic Protein Expression
- Protein Expression Approaches
- Cell-Free Protein Expression
- E.coli Protein Expression
- Yeast Protein Expression
- 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
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.
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
- Competent Cell Product Comparison
- 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.