Cathepsin G, Human Neutrophil

General description

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.

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. Inhibited by chymostatins, DFP and Z-Phe-CH₂Br.

Note: 1 mU = 1 milliunit.

Warning

Toxicity: Standard Handling (A)

Unit Definition

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.

Preparation Note

Prepared from blood that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Reconstitution

Following reconstitution, aliquot and freeze (-70°C) for long term storage or refrigerate (4°C) for short term storage. Stock solutions are stable for up to 1 week at 4°C or for up to 6 months at -70°C.

Reconstitute in 50 mM NaOAc and 150 mM NaCl, pH 5.5.

Other Notes

Glusa, E., and Adam C. 2001. Por. J. Pharmacol.133, 422.
Shamamian, P., et al. 2001. J. Cell Physiol.189, 197.
Groutas, W.C., et al. 1993. Biochem. Biophys. Res. Commun.197, 730.
Stone, P.J., et al. 1993. Biochem. Biophys. Res. Commun.197, 130.
Groutas, W.C., et al. 1992. Arch. Biochem. Biophys.294, 144.
Maison, C.M., et al. 1991. J. Immunol.147, 921.
Travis, J. 1988. Am. J. Med.84, 37.

Legal Information

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