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Bacterial expression of human cysteine proteinase inhibitor stefin A
D Fong1, T Kartasova, B F Sloane
1Department of Biological Sciences and Bureau of Biological Research, Rutgers, State University of New Jersey, Piscataway 08855-1059.
Abstract:
Stefin A, a cysteine proteinase inhibitor of the cystatin superfamily, has been found to be most abundant in epidermal cells. In order to determine its cellular function, we have expressed human stefin A in Escherichia coli using plasmid expression vectors under the control of bacteriophage T7 RNA polymerase. The heat-stable, antibody-positive bacterial product was isolated using a papain-Sepharose affinity column and was shown to inhibit two cysteine proteinases, papain and human cathepsin B. Recombinant stefin A may have commercial and therapeutic potential in situations requiring inhibition of cysteine proteinase activities, and in cosmetics, as an ingredient in skin creams.