Growth hormone as a drug product that is not limited to its application to the topic of short-term treatment of pediatric patients is made recombinantly. Since the low expression of this heavy protein in the recombinant state influences its effective extraction, various changes have been made on this protein in the culture and expression stage. In this study, optimization based on the concentration of DMSO additive in culture medium, incubation temperature and induction concentration were investigated. The results of PAGE-SDS showed a good percentage for 1% dimethyl sulfoxide and a suitable temperature for incubation of 16 ° C and an appropriate concentration for Isopropylthiogalactoside inducer 0.1 mM. In the next step, the culture specimen was optimized with native gel and dual display (CD) and Visible-UV, and confirmed the expression and production of recombinant protein.
