Miropin (Tannerella forsythia serine protease inhibitor)
Miropin is a prokaryotic serpin (SErine Protease INhibitor) protein from Tannerella forsythia, a human pathogen involved in the pathogenesis of periodontitis. Miropin can inhibit the activity of a broad range of proteases including trypsin, cathepsin G, neutrophil and pancreatic elastases. Therefore, miropin is a unique serpin in its wide range of inhibitory activity. Recombinantly produced in insect cell culture and purified by chelated metal affinity chromatography. Contains a 8X-Histidine tag at the N terminus for purification. This recombinant miropin inhibits the activity of human neutrophil elastase in vitro. At least 95% pure as determined by SDS-PAGE.
1. Ksiazek, M., Mizgalska, D., Enghild, J.J., Scavenius, C.,Thogersen, I.B., and Potempa, J. Miropin, a Novel Bacterial Serpin from the Periodontopathogen Tannerella forsythia, Inhibits a Broad Range of Proteases by Using Different Peptide Bonds within the Reactive Center Loop. (2015) J. Biol. Chem. 290: 658-670.