The great advantages of prokaryotic expression system for recombinant proteins

Prokaryotic expression system is developing well and the process is simple and fast. It has the advantages of low cost and high yield and is worthy trying for most proteins. It is especially suitable for eukaryotic proteins which express prokaryotic sources and don't require post-translational modification.

The necessary host bacteria of prokaryotic expression system include E.coli, Bacillus and the like. Wherein the Gram-positive Bacillus is more suitable to secrete and express recombinant proteins such as recombinant human proteins in its periplasmic space; gram-negative E.coli is capable of expressing heterologous proteins at broad spectrum.

E. coli expression system is currently the most developed recombinant protein expression system. Common strains of E. coli include BL21 (DE3), BL21 (DE3) Star, and B834 (DE3) and so on. All these strains were knocked out protease and are lysogenic to phage DE3. DE3 is a derivative λ phage with a phage resistance zone 21 and / ac / gene, / acUV5 promoter and T7 RNA polymerase gene. This section is inserted into the int gene, thus preventing DE3 from integrating into the chromosome or being excised from the chromosome in the absence of helper phage. Once forming DE3 lysogen state, only /acUV5 promoter induced by IPTG guides T7 RNA polymerase gene transcription. Add IPTG-induced T7 RNA polymerase production in lysogen culture system and then target DNA on plasmid begins to transcribe.

At the same time, there are some specially-designed strains expressing recombinant proteins with special needs. For example, methionine auxotroph expresses selenomethionine proteins; strains with enhancement of solubility express toxic protein expression strains; strains supplemented with rare codons express eukaryotic proteins. And here I would recommend a biocompany named Flarebio which produces and provides superior recombinant proteins including recombinant Cdh10 at competitive prices.