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Catalytic Domain of Human MMP-12

$795.00

Catalog Number: B2011081 (10 µg)
Catalytic Domain of Human MMP-12 is a highly pure recombinant human MMP-12 (catalytic domain 106-267) expressed in E. coli. This product has been used as molecular tool for various chemical, biochemical and immunological applications. It has also been used in a wide array of other biochemical and immunological applications. Custom bulk amounts of this product are available upon request.

Live enquiry about this product via Text/SMS: 1-858-900-3210.

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SKU: B2011081 Categories: ,

Description

Catalytic Domain of Human MMP-12
Catalog number: B2011081
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 10 µg
Molecular Weight or Concentration: na
Supplied as: Solution
Applications: molecular tool for various chemical, biochemical and immunological applications
Storage: -20 °C
Keywords: MMP-12
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

References:
1: Van Doren SR. Matrix metalloproteinase interactions with collagen and elastin Matrix Biol. 2015 May-Jul;44-46:224-31.
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.
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.
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.
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.
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.
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.
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.
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.
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.

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