The news correspondents obtained a quote from the research from AECS, "In this work, a plasmid, pRSET-TEV-rhGH, has been constructed to overexpress recombinant human GH (rhGH) by cloning its gene downstream of an N-terminal 6x His-tagged polypeptide (43 aa) in the 17 promoter-plasmid pRSET. This polypeptide was cleavable by means of the integrated recognition site for the tobaccos etch virus (TEV) protease, resulting in an rhGH protein at an exact length and sequence. After IPTG induction, this plasmid effectively expressed TEV-rhGH protein (27 kDa) in the cytoplasm of Escherichia coil, which accumulated in the form of inclusion bodies. The 6 x His-tagged protein, with a yield of similar to 150 mg/L of culture, was purified from the cell extract using metal affinity chromatography, as shown after SDS-PAGE blue staining, and was confirmed by immunoblotting using specific commercial monoclonal antibodies. In order to detect TEV-rhGH, in ELISA and immunoblotting, specific polyclonal antibody, with high titer (similar to 10(-5) fold dilution), was produced in a rabbit and purified using affinity chromatography."
According to the news reporters, the research concluded: "Preliminary tests have proved that TEV-rhGH protein and its specific purified IgG antibody could provide valuable tools for rhGH productive and diagnostic purposes."
For more information on this research see: Prokaryotic overexpression of TEV-rhGH and characterization of its polyclonal antibody. Gene, 2014;542(1):69-76. Gene can be contacted at: Elsevier Science Bv, PO Box 211, 1000 Ae
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