Interferon alpha 2b gene (INF α2b) as a protein with antiviral and antitumor activities is potentially a valuable therapeutic proteins to work on. Prior to a large scale production of the target protein, it is recommended to examine it in an experimental scale, so that bacterial host could be a proper choice as it leads us to a deep insight of the subject. In this research, INF α2b sequence obtained from NCBI gene data bank, and after optimization it was subjected to be cloned and expressed in pET28a+. In order to primary examination of the target protein, Escherichia coli was considered as a prokaryotic expression system. IPTG induction of the protein in bacteria cells containing the construct pET: IFN, followed by resolving total proteins through SDS-PAGE. The expected size of the investigated protein, about 24kDa, observed through gel separation. Further assessment via western blotting confirmed successful expression of IFN α2b.

Concentrating on the interferon alpha 2b gene (INF 2b), a protein having antiviral and anticancer properties, could be beneficial therapeutically. It is advised to conduct an experimental examination of the target protein before having it produced on a big scale. The bacterial host is a good option since it allows us to gain a thorough understanding of the topic. The INF-2b sequence used in this study was obtained from the NCBI gene data library, and following optimization, it was cloned and expressed in pET28a+.Escherichia coli was chosen as the prokaryotic expression system for the target protein's initial analysis. Bacterial cells expressing the pET:IFN construct were IPTG-induced to produce the protein, which was then resolved using SDS-PAGE. During gel separation, the studied protein's anticipated size of roughly 24 kDa was seen. IFN 2b was successfully expressed, according to further evaluation by western blotting.