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  MMP-3, Proenzyme, Human, Recombinant
Cat. No. PF063  
All Categories » Calbiochem » Proteins and Enzymes » Proteases » Matrix Metalloproteinases (MMP)

Lyophilized. Lyophilized from 100 mM NaCl, 50 mM HEPES, pH 7.3. AVOID FREEZE/THAW CYCLES. Recombinant, human pro-MMP-3 purified from cell culture supernatant. May be used as a positive control or standard for zymographic analysis, or substrate assay. Requires activation for immunoblotting, prior to use. M.W. 57000/58000. Activity: The activity of proenzyme MMP 3 was measured by substrate cleavage assay using 0.5 mM thiopeptiolide (Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-Oet) as a substrate. The activity was also assessed by degradation of a peptide substrate (DNP-PYAYWMR) using activated MMP-3 as measured by HPLC.. Purity: ≥95% by SDS-PAGE. EC 3.4.24.17.

Ref.: Sole, S., et al. 2004. J. Neuropathol. Exp. Neurol. 63, 338. Galazka, G., et al. 1996. Biochem. 35, 11221. Cottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861. Stetler-Stevenson, W.G., et al. 1993. FASEB J. 7, 1434. Netzel-Arnett, S., et al. 1991. Anal. Biochem. 195, 86. Woessner, J.F. 1991. FASEB J. 5, 2145. Liotta, L.A. and Stetler-Stevenson, W.G. 1990. In Seminars in Cancer Biology, ed. M.M. Gottesman. Vol. 1, 99. Zymography References Xia, T., et al. 1996. Biochim. Biophys. Acta. 1293, 259. Kleiner, D.E. and Stetler-Stevenson W.G. 1994. Anal. Biochem. 218, 325. Heussen, C. and Dowdle, E.B. 1980. Anal. Biochem. 102, 196. Substrate Cleavage Assay References Xia, T., et al. 1996. Biochim. Biophys. Acta. 1293, 259. Netzel-Arnett, S., et al. 1991. Anal. Biochem. 195, 86.

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SolubilityMolecular FormulaMol. Wt.
H2 57000 

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PF063: MMP-3, Proenzyme, Human, Recombinant - English
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All Categories » Calbiochem » Proteins and Enzymes » Proteases » Matrix Metalloproteinases (MMP)