Expression And Purification Of Recombinant TRAIL Expressed In Escherichia Coli

Antineoplastic drugs have always been the focus of drug research.In the field of biopharmaceuticals,TNF-related apoptosis-inducing ligand(TRAIL)is one of the research hotspots.As early as in 1995,TRAIL was found and belonged to the TNF family.Compared with other INF members,its greatest advantage in drug treatment is the selective induction of apoptosis in tumor cells,while having no toxic or side effects on normal cells.Studies have shown that when TRAIL is combined with other anti-cancer drugs,it can have a better therapeutic effect,reduce the frequency of drug injections,and improve patient compliance.In this thesis,TARIL was expressed in E.coli.and purified through gene recombination technology.We investigated inclusion bodies and excreted form during the process the TRAILsynthesis,and the fermentation process was optimized for increasing the expression level.Furthermore,various purification methods were studied.Finally,the optimum TRAIL production process was established.The purity of the target protein exceeded 95%.