Takara Recombinant protein expression: Brevibacillus Expression System II

Overview

• Efficient production of secreted or intracellular recombinant target proteins
• Negligible amounts of extracellular protease; products remain intact in culture medium
• Unlike E. coli, no endotoxins
• Proteins are produced in active form
• Easy to culture, handle, and sterilize

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Examples of Proteins Expressed Using the Brevibacillus Expression System II

High expression levels have been achieved for a variety of proteins (enzymes, antigens, and cytokines) regardless of their genetic origin (bacterial, archaeal, or eukaryotic).
Because secreted eukaryotic proteins often depend on intact disulfide bonds for activity, it is generally difficult to produce active proteins using typical prokaryote-based expression systems.
However, due to the secretory advantages of the Brevibacillus Expression System II, high expression levels of active recombinant proteins are possible even for proteins with extensive disulfide bonds.

References

• Takagi, H., Kadowaki, K. & Udaka, S. Screening and characterization of protein-hyperproducing bacteria without detectable exoprotease activity. Agric. Biol. Chem. 53, 691–699 (1989).

Product Citations

• Mizukami, M., Hanagata, H. & Miyauchi, A. Brevibacillus Expression System: Host-Vector System for Efficient Production of Secretory Proteins. Curr. Pharm. Biotechnol. 11, 251–258 (2010).
• Sugimoto, S. et al. Cloning, expression and purification of extracellular serine protease Esp, a biofilm-degrading enzyme, from Staphylococcus epidermidis. J. Appl. Microbiol. 111, 1406–1415 (2011).
• Takano, T. et al. Expression of the Cycledextrin Glucanotransferase Gene of Bacillus macerans in Bacillus brevis. Biosci. Biotech. Biochem. 56, 808–809 (1992).
• Teramura, N. et al. Cloning of a Novel Collagenase Gene from the Gram-Negative Bacterium Grimontia (Vibrio) hollisae 1706B and Its Efficient Expression in Brevibacillus choshinensis. J. Bacteriol. 193, 3049–3056 (2011).
• Tojo, H. et al. Production of human protein disulfide isomerase by Bacillus brevis. J. Biotechnol. 33, 55–62 (1994).
• Yamagata, H., Nakahama, N., Suzuki, Y., Tsukagoshi, N. & Udaka, S. Use of Bacillus brevis for efficient synthesis and secretion of human epidermal growth factor. Proc. Natl. Acad. Sci. USA. 86, 3589–3593 (1989).
• Yamamoto, A., Fujino, M., Tsuchiya, T. & Iwata, A. Recombinant canine granulocyte colony-stimulating factor accelerates recovery from cyclophosphamide-induced neutropenia in dogs. Vet. Immunol. Immunopathol. 142, (2011).
• Yamamoto, A., Iwata, A., Saito, T., Watanabe, F. & Ueda, S. Expression and purification of canine granulocyte colony-stimulating factor (cG-CSF). Vet. Immunol. Immunopathol. 130, 221–225 (2009).
• Yashiro, K. et al. High-Level Production of Recombinant Chicken Interferon-γ by Brevibacillus choshinensis. Protein Expr. Purif. 23, 113–120 (2001).

Additional Product Information

Please refer to the product’s Certificate of Analysis for details on storage conditions, components, and technical specifications.
Kit Components Lists and Certificates of Analysis are available under the Documents tab.