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.
Protein Expression & Purification includes these areas of focus:
- Protein Expression Approaches
- E.coli Protein Expression
- Yeast Protein Expression
- Cell-Free Protein Expression
- Coupled Protein Expression & Purification
- Maltose Binding Protein Expression
- IMPACT™ Protein Expression
- His-tagged Protein Expression
- Yeast Chitin Binding Domain Tag
- Expression of Difficult Proteins
- Toxic Protein Expression
- Membrane Protein Expression
- Disulfide-Bonded Protein Expression
- Affinity Purification
FAQs for Protein Expression & Purification
Protocols for Protein Expression & Purification
- Co-expression of Multiple Proteins in Kluyveromyces lactis
- E. coli Lemo21(DE3)
- 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
Competent Cells Brochure
The Competent Cell brochure provides information on the different competent cell strains for cloning and protein expression available from NEB.
Protein Expression & Purification Brochure
The Protein Expression and Purification brochure provides information on the advanced tools for protein expression and purification offered by NEB.
- Bypassing Common Obstacles in Protein Expression
- The Next Generation of Cell-free Protein Synthesis
- Why Choose the K. lactis Protein Expression Kit?
- Competent Cell Product Comparison
- Protein Expression and Purification Selection Chart
- Convenient Formats of Competent Cells
Other Tools & Resources
While NEB develops and validates its products for various applications, the use of this product may require the buyer to obtain additional third party intellectual property rights for certain applications.
For more information about commercial rights, please contact NEB's Global Business Development team at firstname.lastname@example.org.
This product is intended for research purposes only. This product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
NEB has a long history in recombinant protein expression and has developed a wide array of solutions for proteins that are difficult to express.