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MMP-13 (catalytic domain) (human), (recombinant)

 
BML-SE246-0010 10 µg 384.00 USD
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Product Specification

Alternative Name:Matrix metalloproteinase 13, Collagenase-3
 
MW:20.4 kDa
 
Source:Produced in E. coli. Active Matrix Metalloproteinase-13 (MMP-13, collagenase-3) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-13 (Tyr104-Asn274, NM_002427) with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-13 which lacks the C-terminal hemopexin domain. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected.
 
UniProt ID:P45452
 
Formulation:Liquid. In 50mM TRIS, 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 0.5% Brij-35, and 30% glycerol.
 
Purity:≥95% (SDS-PAGE)
 
Purity Detail:Purified by multi-step chromatography.
 
Activity:Preincubation of MMP-13 catalytic domain at 13nM with the broad-spectrum inhibitor GM6001 (Prod. No. BML-EI300) at 20nM for 1 hour completely inhibits enzymatic activity.
 
Specific Activity:≥100 U/µg. One U=100 pmol/min at 37°C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt (100 µM; Prod. No. BML-P125) as substrate.
 
Application Notes:Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
BML-SE246 SDS-PAGE
SDS-PAGE Analysis: Lane1: MW Marker; Lane 2: 2µg of purified MMP-13 (catalytic domain) (human), (recombinant).
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BML-SE246 SDS-PAGE

Product Literature References

Enzymatic, physicochemical and biological properties of MMP-sensitive alginate hydrogels: K.B. Fonseca, et al.; Soft Matter 9, 3283 (2013),
Development and validation of novel enzyme activity methods to assess inhibition of matrix metalloproteinases (MMPs) in human serum by antibodies against enzyme therapeutics: T.J. Edkins, et al.; J. Pharm. Biomed. Anal. 70, 408 (2012), Abstract;
Directed evolution of protease beacons that enable sensitive detection of endogenous MT1-MMP activity in tumor cell lines: A. Jabaiah, et al.; Chem. Biol. 18, 392 (2011), Abstract; Full Text
The in vitro resistance of IgG2 to proteolytic attack concurs with a comparative paucity of autoantibodies against peptide analogs of the IgG2 hinge: R.J. Brezski, et al.; Mabs 3, 558 (2011), Abstract; Full Text
The effect of a hydroxamic acid-containing polymer on active matrix metalloproteinases: G.A. Skarja, et al.; Biomaterials 30, 1890 (2009), Abstract;

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