Product Details
| Alternative Name: | Matrix metalloproteinase 8, Neutrophil collagenase, Collagenase-2 |
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| MW: | 20.3 kDa |
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| 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. |
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| UniProt ID: | P22894 |
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| Formulation: | Liquid. In 50mM TRIS, 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 0.5% Brij-35, and 30% glycerol. |
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| Purity: | ≥90% (SDS-PAGE) |
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| Purity Detail: | Purified by multi-step chromatography. |
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| 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. |
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| 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. |
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| Application Notes: | Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Regulatory Status: | RUO - Research Use Only |
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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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