Salt-free lyophilized solid. Native cathepsin G from human neutrophil. A serine protease that degrades collagen and proteoglycans. Has been implicated in connective tissue diseases such as emphysema and rheumatoid arthritis. Acts as a potent agonist of human platelet activation leading to their aggregation. Reported to be involved in the activation of pro MMP-2 via mechanism requiring MT1-MMP. Inhibited by chymostatin, DFP, and Z-Phe-CH₂Br. Reconstitute in 150 mM NaCl, 50 mM sodium acetate buffer, pH 5.5. Specific activity: ≥2 units/mg protein. One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol of Suc-AAPF-pNA per min at 25°C, pH 7.5. Purity: ≥95% by SDS-PAGE. Prepared from blood that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV. pH optimum 7.5. EC 3.4.21.20, CAS 107200-92-0. Note: 1 mU = 1 milliunit.

Merck Index: 14, 1905
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