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  MMP-2, Proenzyme, Human, Recombinant, CHO Cells
Cat. No. PF037  
All Categories » Calbiochem » Proteins and Enzymes » Proteases » Matrix Metalloproteinases (MMP)

72 kDa Gelatinase
Gelatinase A
Matrix Metalloproteinase 2

Liquid. In 150 mM NaCl, 20 mM Tris-HCl, 5 mM CaCl2, 0.05% BRIJ®-35 Detergent, pH 7.4. AVOID FREEZE/THAW CYCLES. Recombinant, human pro-MMP-2 expressed in CHO cells. Can be used as a positive control for zymographic analysis, immunoblotting, and substrate cleavage assay. A portion (less than 10%) of the enzyme may be seen as a naturally-occurring dimer. Dimerization does not interfere with activation. May contain up to 10% TIMP proteins. During storage, a small portion (less than 10%) of the enzyme may also become activated. Activity: Measured by its ability to degrade gelatin using zymography. 1 ng of enzyme is sufficient to visualize degraded gelatin by coomassie blue stain in zymography. Activated rhMMP-2 degrades type IV collagen, as visualized by SDS-PAGE and cleaves the coumarin peptide substrate, (7-methoxycoumarin-4-yl) Acetyl-Pro-Leu-Gly-Leu-(3-[2, 4-dinitrophenyl-L-2, 3-diaminopropionyl)-Ala-Arg-NH2 (Cat. No. 03-32-5032), as measured by fluorescence (excitation at 320 nm and emission at 405 nm).. Purity: ≥90% by SDS-PAGE. EC 3.4.24.24.

Ref.: Buisson-Leqendre, N., et al. 2004. Arth. Rheumat. 50, 2151. 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. Neurosci. Lett. 201, 223. 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. 462. Kleiner, D.E. and Stetler-Stevenson W.G., 1994. Anal. Biochem. 218, 325. Zempo, N., et al. 1994. J. Vasc. Surg. 20, 209. Birkedal-Hansen, H. 1993. J. Periodontol. 64 474. 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 & C.V. Gay, Eds. 290. Jeffrey, J.J. 1992. In Wound Healing: Biochemical and Clinical Aspects. R.F. Diegelmann and W.J. Lindblad, Eds. 177. 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. Heussen, C. and Dowdle, E.B., 1980. Anal. Biochem. 102, 196.

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  72000 

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PF037: MMP-2, Proenzyme, Human, Recombinant, CHO Cells - English
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Related Categories:
All Categories » Calbiochem » Proteins and Enzymes » Proteases » Matrix Metalloproteinases (MMP)

Selected Citations:
  1. Feng Zheng, et al. (2004) Development of albuinuria and glomerular lesions in normoglycemic B6 recepients of db/db mice bone marrow. Diabetes 53, 2420-2427.
  2. William J. Lane, et al. (2000) Stromal-derived factor 1-induced megakaryocyte migration and platelet production is dependent on matrix metalloproteinases. Blood 96, 4152-4159.