The Bacillus megaterium expression system provides a versatile and easy-to-handle tool for stable and high-yield protein production, both small- and large-scale.
B. megaterium has proven to be an excellent host for the expression of non-homologous DNA. Unlike other bacilli strains, none of the alkaline proteases are present. This enables cloning and expression of foreign proteins without degradation.
In addition, there are no endotoxins found in the cell wall. B. megaterium can stably maintain several extra-chromosomal DNA elements in parallel. Protein yields are exceptionally high, even if inexpensive substrates are used.
The high-performance (hp) BMEG vectors offer yields up to 10-fold higher than the basic plasmids. The hp vectors include vectors carrying two different signal peptide sequences, a 6xHis-tag, a Strep-tag, or two ribosome binding sites for simultaneous dual expression. Vectors encoding C- or N-terminal His-tags for easy purification are also offered. The protein secretion with LipA or YocH signal peptides is up to 9-fold increased. All hp BMEG vectors have established multiple cloning sites for versatile cloning. Induction of protein expression is achieved by the tightly regulated and efficiently inducible xylose operon.
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