Bacterial Expression Platform

Large-scale production of recombinant proteins can be achieved in many expression systems. Bacterial expression systems offer the advantages of fast growth, well-characterized genetics, confirmed safety background, and high protein yield, making them one of the most important industrial expression hosts.

Bacterial Protein Expression Workflow

Bacterial Expression Platform

  • Gene synthesis and codon optimization
  • Vector construction
    • Cloning cDNA into expression vectors
    • Plasmid sequencing
    • Plasmid preparation
  • Protein expression testing
    • Bacterial strain transformation
    • Pilot expression and purification trial
    • Protein expression evaluation (SDS-PAGE)
  • Scalable expression and purification
    • Soluble protein purification
    • Protein refolding and purification (inclusion bodies)
  • Large-scale expression and purification
  • QC analysis (SDS-PAGE, UV, etc)

E. coli Expression Platform

E. coli serves as an attractive host system due to its well-characterized genetic background, high yield capacity, robust production cycle, strong anti-pollution abilities, and ease of scaling. Creative Biogene offers one-stop services for high-quality E. coli protein expression, with abundant experience in soluble protein expression and production and in protein refolding. We also offer extensive protein production and purification services tailored to your specific requirements, including endotoxin removal, tag removal, and protein labeling. Our E. coli cell culture in animal-free conditions, can be used to facilitate drug development. Pilot-scale production is available to enable the fast screening of therapeutic protein candidates.

B. subtilis Expression Platform

B. subtilis is a nonpathogenic bacterium that can efficiently secrete large quantities of a variety of enzymes into the culture medium. Such secretion facilitates further purification steps and simplifies product recovery. Many Processes concerning production technology and large-scale fermentation using this bacterium is very well acquainted. The major advantage of B. subtilis is that it does not produce LPS, and it has no significant bias in codon usage.

Other Options for Bacterial Expression System


Bacterial Expression for Therapeutic Proteins Production

Most therapeutic proteins are naturally glycosylated with either N- or O-linked glycans, these being the most common and structurally complex natural post-translational modifications (PTMs). Different expression systems can yield glycoproteins with quite different glycoform profiles. Hence, to produce biologically relevant, human compatible glycan structures, the expression systems to produce therapeutic glycoproteins must be carefully chosen. Bacterial reducing environment makes disulfide bond formation challenging, and the fact that they do not naturally produce N- or O-glycosylated products limits their utility. Advanced cellular engineering approaches have improved the expression of human proteins in bacteria with an oxidizing cytoplasmic environment. Our commercial strains also contain constitutively expressed, cytoplasmic, disulfide bond isomerase (DsbC) to aid in the formation of disulfide bonds and promote proper protein folding.

Creative Biogene's bacterial expression platform comprises an extensive collection of plasmids and host strains. We can provide excellent construct design strategies to our clients, to obtain high-quality recombinant proteins. Multiple fusion tags are also available to meet specific needs for protein purification and characterization. Our experts can help the client troubleshoot and solve various issues during protein purification, such as increasing purity and column binding, refolding, and formulation.

If you are interested in our services, please contact us for more details.


  1. Du, Ting; Buenbrazo, Nakita; Kell, Laura; Rahmani, Sadia; Sim, Lyann; Withers, Stephen G.; DeFrees, Shawn; Wakarchuk, Warren. A Bacterial Expression Platform for Production of Therapeutic Proteins Containing Human-like O-Linked Glycans. Cell Chemical Biology. 2018.
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