Abstract:

Recombinant interferon beta (RIFN-β) proteins are used in ecaryotic and procaryotic expression systems with similar processes for the production of RIFN-β1a and RIFN-β1b. Difficulty in the purification of rIFN-β1a produced by eukaryotic expression systems and the impact of biological activity strengthens the production of recombinant protein with these processes. In the production of procaryotic expression systems, rIFN-β1b has been found to have fewer purification and activity problems. The better use of the product’s secretion properties found in Escherichia coli from prokaryotic bacteria shows that this system will be more preferred in the production of rIFN-β1b. If the structure is designed to be dissolved out of the residential cell they produce, it is expected that E. coli residential cells will not break down during purification to facilitate the purification processes. The use of E. coli in the production of RIFN-β1b proteins, which has type I and type II secretion system, is expected to reduce purification and activity problems in the out-of-cell secretion of RIFN-β1b produced in this reservoir, and also to eliminate the toxic effect that RIFN-β1b will make to the reservoir cell. For this purpose E. In order to remove the disadvantages in the coli production system, a variety of approaches are designed, including the process of the discharge of rIFN-β1b proteins outside the cell by transferring the DmsA signal peptide to the pET22b expression vector, as well as the PelB signal peptide. In this collection, the information based on the characteristics of IFNs, the clinical applications of RIFN-β and the research on the methods of production of RIFN-β1b and the information on the use of signal peptides in the process of production of RIFN-β1b in the E. coli residential cells.

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