Production and characterization of a monoclonal antibody against Schistosoma japonicum glutathione S-transferase.
Schistosoma japonicum glutathione S-transferase (GST), expressed from a pGEX plasmid, was isolated from Escherichia coli cells and used to immunize mice in order to generate specific anti-GST monoclonal antibodies. Using a modified immunization and fusion procedure, one stable hybridoma clone secreting an anti-GST antibody (alpha GST-1) was obtained. Milligram quantities of this antibody were produced in vitro in a miniPERM bioreactor and subsequently purified by protein G affinity chromatography. The characteristics of this antibody were investigated by enzyme-linked immunosorbent assays and immunoblotting experiments. The alpha GST-1 antibody was found to react specifically with GST and GST fusion proteins and demonstrated no reactivity with normal E. coli proteins. This monoclonal antibody should be a valuable reagent for tracing the production of GST fusion proteins and possibly for affinity purification of GST fusion proteins.[1]References
- Production and characterization of a monoclonal antibody against Schistosoma japonicum glutathione S-transferase. Campbell, M.J., McFall, P., Niederhuber, J.E. J. Immunol. Methods (1995) [Pubmed]
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