The authors of the publication below utilized human cathepsin G, human tissue plasminogen activator, >85% single chain, and active mouse urokinase, HMW from Molecular Innovations.
“We characterized four serpins from the liver fluke Fasciola hepatica. Biochemical characterization revealed that recombinant FhS-2 inhibits the activity of human neutrophil cathepsin G, while recombinant FhS-4 inhibits the activity of bovine pancreatic chymotrypsin and cathepsin G. Consistent with inhibitor function profiling data, FhS-4 inhibited cathepsin G-activated platelet aggregation in a dose-responsive manner.”
A variety of proteases including cathepsin G, tPA, and uPA were incubated with a molar excess of recombinant F. hepatica serpins followed by measurement of residual protease activity using enzyme appropriate chromogenic substrates. Cathepsin G was preincubated with recombinant FhS-4 before addition to bovine platelet rich plasma for platelet aggregation assays.
