Purification of recombinant Schistosoma japonicum protein SjGST and preparation and characterization of the monoclonal antibody

Objective: To isolate and purify recombinant Schistosoma japonicum (Chinese strain) protein glutathione S-transferase (rSjGST) for preparing the monoclonal antibodies (McAbs) against rSjGST.Methods: Balb/c mice were immunized with purified rSjGST protein.The anti-rSjGST monoclonal antibody was obtained through hybridoma technique.Characterization of the antibody was performed by ELISA and Western blot analysis.Results: The data had shown that high purified rSjGST protein and the hybridoma cell line 3C12 secreting McAbs against rSjGST protein were obtained.The subclass of McAbs was confirmed to be IgG1.Conclusions: The rSjGST protein was induced to express by isopropy-β-D-thiogalactoside in prokaryotic hosts Escherichia coli with high efficiency and its antibodies were harvested.They can be applied to further study on immunodiagnostic methods of Schistosoma japonicum.