Gelatinase A
Active Matrix Metalloproteinase 2 Liquid. In 50 mM HEPES, 10 mM CaCl2, 20% glycerol, 0.005% BRIJ®-35 Detergent, pH 7.5. AVOID FREEZE/THAW CYCLES. Full-length, recombinant, human pro-MMP-2 expressed in CHO cells that is subsequently activated by APMA. APMA is removed through a desalting column. The substrate specificity for MMP-2 includes collagen (types IV, V, VII, and X), elastin, and gelatin (type I). The presence of TIMP-2 inhibitor prevents degradation of the MMP-2 C-terminal regulatory domain. TIMP-2 is also an inhibitor of proteolysis and will inhibit the activity of the enzyme. Useful for immunoblotting, substrate cleavage assay and zymography. Activity: DA412/hour/µg protein: ≥ 8.0 in standard thiopeptolide hydrolysis assays.. Purity: ≥90% by SDS-PAGE; contains 9% TIMP-2. EC 3.4.24.24. Ref.: Liepnisch, E., et al. 2003. J. Biol. Chem. 278, 25982. Parsons, S.L., et al. 1997. Br. J. Surg. 84, 160. Backstrom, J.R., et al. 1996. J. Neuro. 16, 7910. Lim, G.P., et al. 1996. J. Neurochem. 67, 251. Xia, T., et al. 1996. Biochim. Biophys. Acta 1293, 259. Chandler, S., et al. 1995 Neuroscience Letters 201, 226. Sang, Q.X., et al. 1995. Biochim. Biophys. Acta 1251, 99. Kenagy, R.D. and Clowes, A.W. 1994. In Inhibition of Matrix Metalloproteinases: Therapeutic Potential. Greenwald, R.A. and Golub L.M., Eds, 465. Zempo, N., et al. 1994. J. Vasc. Surg. 20, 217. Birkedal-Hansen, H. 1993. J. Periodontol. 64, 484. Stetler-Stevenson, W.G., et al. 1993. FASEB J. 7, 1434. Delaisse, J-M. and Vaes, G. 1992. In Biology and Physiology of the Osteoclast. B.R. Rifkin and C.V. Gay, Eds., 290. Jeffrey, J.J. 1992. In Wound Healing: Biochemical and Clinical Aspects. R.F. Diegelmann and W.J. Lindblad, Eds., 194. Jeffrey, J.J. 1991. Semin. Perinatol. 15, 118. Liotta, L.A., et al. 1991. Cell 64, 327. Harris, E. 1990. N. Engl. J. Med. 322, 1277. |
