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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 efficientlyand 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.

Technical Data:


  • 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
Expression vector
» pNY326 DNA 10 µg
» pNCMO2 DNA 10 µg
Control vector
» pNY326-BLA DNA 1 µg
Competent Cells
» Brevibacillus choschinesis competent cells 100 µL x 10 tubes


This product requires completion of a License Agreement before purchase.

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

Proteins Origins Production (g/L) References
α-amylase B. licheniformis 3.7
Sphingomyelinase B. cereus 3.0
Xylanase B. halodurans 0.2
CGTase B. macerans 1.5 2
Chitosanase B. circulans 1.4
Hyper thermo-stable protease A. pernix 0.1
Hyper thermo-stable nuclease P. horikoshii 0.7
PDI human 1.0 3
Surface antigen E. rhusiopathiae 0.9
Surface antigen T. pallidum 0.8
EGF human 1.5 4
NGF mouse 0.2
IFN-γ chicken 0.5 5
TNF-α bovine 0.4
GM-CSF bovine 0.2
GH flounder 0.2

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