A Conventional Method for Fermentation and Purification of Recombinant Human Interleukin 24 from E. coli

Recombinant human interleukin 24 is a member of cytokine family. Recombinant human interleukin 24 is well known as human biological beneficial protein. Recombinant human interleukin 24 production from E.coli with a conventional method is a step to produce a low amount of recombinant protein for characterization and biological properties. The expression of eukaryotic proteins in E. coli leads to formation of insoluble inclusion bodies (IBs). Inclusion bodies solubilization and refolding is a key challenge for active therapeutic protein production. The recovery of recombinant human interleukin 24 from inclusion bodies is a bottle neck of downstream processing. Protein purification not only increases the final product but also improves the quality of final product. In current research work, we practiced the conventional method for production and purification of recombinant human interleukin 24. The fermentation strategy was based on application of LB media for batch culture. The high pressure homogenizer was used for cell lyses. Traditional approach for IB solubilization and refolding was applied to produce a low sample volume for purification. The anion & cation exchange complex chromatography was applied to remove impurities from the sample and to produce purified product. According to conventional method a negligible recombinant human interleukin 24 was produce with more effort and more time consumption.