Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system.

ABSTRACT: Proteins are now widely produced in diverse microbial cell factories. The Escherichia coli is still the dominant host for recombinant protein production but, as a bacterial cell, it also has its issues: the aggregation of foreign proteins into insoluble inclusion bodies is perhaps the main limiting factor of the E. coli expression system. Conversely, E. coli benefits of cost, ease of use and scale make it essential to design new approaches directed for improved recombinant protein production in this host cell. With the aid of genetic and protein engineering novel tailored-made strategies can be designed to suit user or process requirements. Gene fusion technology has been widely used for the improvement of soluble protein production and/or purification in E. coli, and for increasing peptid

SUBMITTER: Costa S 

PROVIDER: S-EPMC3928792 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature