Brevibacillus Expression System II
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Brevibacillus choshinensis is a Gram-positive bacterium well-suited for heterologous protein expression. The Brevibacillus Expression System II generates secreted target proteins efficiently1 and is ideal for eukaryotic recombinant protein expression, resulting in a high yield of active protein. TheBrevibacillus system is also almost completely free of proteases, allowing for the production of intact protein products.
The Brevibacillus system facilitates disulfide bond formation, which is often required for activity in proteins of eukaryotic origin. In addition, B. choshinensis serves as an excellent host for intracellular protein production, producing soluble intracellular proteins in the cytoplasm without the formation of inclusion bodies. In fact, the Brevibacillus Expression System II often works better than comparable E. coli-based systems for the expression of certain recombinant protein targets.
Using His-tag vectors (pNC-HisE, pNC-HisF, pNC-HisT, pNI-His) allows for quick and easy purification of the expressed target proteins. These tags can be removed by protease treatment following purification.
- 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
|Brevibacillus Expression System||1 kit|
|» pNY326 DNA||10 µg|
|» pNCMO2 DNA||10 µg|
|» pNY326-BLA DNA||1 µg|
|» Brevibacillus choschinesis competent cells||100 µL x 10 tubes|
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Examples of Proteins Expressed using the Brevibacillus Expression System II
Examples of expressed proteins using the Brevibacillus Expression System II are shown below (see Table 1). High expression levels have been achieved for a variety of proteins (enzymes, antigens and cytokines) regardless of their genetic origin (bacterial, archaeal and 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 BrevibacillusExpression System II, high expression levels of active recombinant protein are possible even for proteins with extensive disulfide bonds.
Table 1. Examples of successful heterologous protein expression using the B. choshinensishost expression system
|Hyper thermo-stable protease||A. pernix||0.1|
|Hyper thermo-stable nuclease||P. horikoshii||0.7|
|Surface antigen||E. rhusiopathiae||0.9|
|Surface antigen||T. pallidum||0.8|