The NEBExpress® MBP Fusion and Purification System takes advantage of the strong Ptac promoter and the translation initiation signals of maltose binding protein (MBP) to enhance solubility and expression levels of a desired protein in E. coli. The resulting product is an MBP fusion protein, which is then purified by affinity chromatography.
- Reliable E. coli expression: substantial yields (up to 100 mg/L)
- Fusion to MBP has been shown to enhance the solubility of proteins expressed in E. coli (1)
- Two-step purification: amylose elution followed by TEV Protease cleavage and Ni resin isolation results in a highly pure tag-free target protein
- Gentle elution with maltose; no detergents or harsh denaturants required
Kapust and Waugh (1999). Protein Science. 8, 1668-1674. (https://doi.org/10.1110/ps.8.8.166)
- What systems does NEB offer for protein expression and purification?
- What strain(s) do you recommend as hosts for the pMAL vectors?
- Can I perform a batch purification using the amylose resin?
- How can TEV Protease be removed from the reaction after cleavage?
- How do I separate MBP and TEV Protease from the protein of interest?
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.
- Protein Expression & Purification Brochure
- Purification Beads, Columns and Resins Brochure
- Protein Expression and Purification Selection Chart
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This webinar shares solutions developed by NEB scientists for producing various classes of protein, including: genetically-tailored E.coli host strains, expression vectors and valuable guidelines for generating properly-folded recombinant protein.