Brevibacillus choshinensis is a Gram-positive bacterium well-suited for heterologous protein expression. The Brevibacillus Expression System II generates secreted target proteins efficiently (Takagi et al. 1989) and is ideal for eukaryotic recombinant protein expression, resulting in a high yield of active protein. The Brevibacillus system is also almost completely free of proteases, allowing for the production of intact protein products.
Brevibacillus choshinensis is a Gram-positive bacterium well-suited for heterologous protein expression. The Brevibacillus Expression System II generates secreted target proteins efficiently (Takagi et al. 1989) and is ideal for eukaryotic recombinant protein expression, resulting in a high yield of active protein. The Brevibacillus system is also almost completely free of proteases, allowing for the production of intact protein products.
The Brevibacillus system facilitates disulfide bond formation, which isoften requiredfor 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 ofinclusion bodies. In fact, the Brevibacillus Expression System II often works better than comparableE. coli-based systemsfor the expression ofcertain recombinant protein targets.
Using his-tag vectors (pNC-HisE, pNC-HisF, pNC-HisT, pNI-His) allowsfor quick andeasypurification of the expressed target proteins. These tags can be removed by protease treatment following purification.
