Catalytic Domain of Human MMP-12

<strong>Catalytic Domain of Human MMP-12</strong>_x000D_ <strong>Catalog number:</strong> B2011081_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 10 µg_x000D_ <strong>Molecular Weight or Concentration:</strong> na_x000D_ <strong>Supplied as:</strong> Solution_x000D_ <strong>Applications:</strong> molecular tool for various chemical, biochemical and immunological applications_x000D_ <strong>Storage:</strong> -20 °C_x000D_ <strong>Keywords:</strong> MMP-12_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Van Doren SR. Matrix metalloproteinase interactions with collagen and elastin Matrix Biol. 2015 May-Jul;44-46:224-31._x000D_ 2: Taddese S, Jung MC, Ihling C, Heinz A, Neubert RH, Schmelzer CE. MMP-12 catalytic domain recognizes and cleaves at multiple sites in human skin collagen type I and type III Biochim Biophys Acta. 2010 Apr;1804(4):731-9._x000D_ 3: Bhaskaran R, Palmier MO, Lauer-Fields JL, Fields GB, Van Doren SR. MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity J Biol Chem. 2008 Aug 1;283(31):21779-88._x000D_ 4: Fulcher YG, Van Doren SR. Remote exosites of the catalytic domain of matrix metalloproteinase-12 enhance elastin degradation Biochemistry. 2011 Nov 8;50(44):9488-99._x000D_ 5: Lamort AS, Gravier R, Laffitte A, Juliano L, Zani ML, Moreau T. New insights into the substrate specificity of macrophage elastase MMP-12 Biol Chem. 2016 May;397(5):469-84._x000D_ 6: Zheng X, Ou L, Tong X, Zhu J, Wu H. Over-expression and refolding of isotopically labeled recombinant catalytic domain of human macrophage elastase (MMP-12) for NMR studies Protein Expr Purif. 2007 Dec;56(2):160-6._x000D_ 7: Bhaskaran R, Palmier MO, Bagegni NA, Liang X, Van Doren SR. Solution structure of inhibitor-free human metalloelastase (MMP-12) indicates an internal conformational adjustment J Mol Biol. 2007 Dec 14;374(5):1333-44._x000D_ 8: Parkar AA, Stow MD, Smith K, Panicker AK, Guilloteau JP, Jupp R, Crowe SJ. Large-scale expression, refolding, and purification of the catalytic domain of human macrophage metalloelastase (MMP-12) in Escherichia coli Protein Expr Purif. 2000 Nov;20(2):152-61._x000D_ 9: Bertini I, Calderone V, Fragai M, Jaiswal R, Luchinat C, Melikian M, Mylonas E, Svergun DI. Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12 J Am Chem Soc. 2008 Jun 4;130(22):7011-21._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/20655856">10: Liang X, Arunima A, Zhao Y, Bhaskaran R, Shende A, Byrne TS, Fleeks J, Palmier MO, Van Doren SR. Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3 Biophys J. 2010 Jul 7;99(1):273-83. </a>_x000D_ _x000D_ <strong>Products Related to Catalytic Domain of Human MMP-12 can be found at</strong> <a href="https://moleculardepot.com/product-category/Proteins/"> Proteins</a>