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MMP-8 (catalytic domain) (human), (recombinant)

BML-SE255-0010 10 µg 506.00 USD
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Product Details

Alternative Name:Matrix metalloproteinase 8, Neutrophil collagenase, Collagenase-2
MW:20.3 kDa
Source:Produced in E. coli. Active Matrix Metalloproteinase-8 (MMP-8, neutrophil collagenase, collagenase-2) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-8 (Phe99-Gln269, NM_002424) with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-8 which lacks the C-terminal hemopexin domain1. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected.
UniProt ID:P22894
Formulation:Liquid. In 50mM TRIS, 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 0.5% Brij-35, and 30% glycerol.
Purity:≥90% (SDS-PAGE)
Purity Detail:Purified by multi-step chromatography.
Activity:Preincubation of MMP-8 catalytic domain at 13.6 nM with the broad-spectrum inhibitor GM6001 (Prod #BML-EI300) at 20nM for 1 hour completely inhibits enzymatic activity.
Specific Activity:≥2000 pmol/min/µg 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:Dry Ice
Long Term Storage:-80°C
Regulatory Status:RUO - Research Use Only

Product Literature References

Mechanical strain modulates extracellular matrix degradation and byproducts in an isoform-specific manner: A. Yeganegi, et al.; Biochim. Biophys. Acta Gen. Subj. 1867, 130286 (2023), Abstract;
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 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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