Product Details
| Alternative Name: | Matrix metalloproteinase 20, Enamelysin |
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| MW: | 19.9 kDa |
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| Source: | Produced in E. coli. Active recombinant matrix metalloproteinase-20 (MMP-20, enamelysin) cloned from human cDNA. The enzyme consists of residues Tyr108-Phe276 (NM_004771), which comprises the catalytic domain of human MMP-20, with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-20 which lacks the C-terminal hemopexin domain. |
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| UniProt ID: | O60882 |
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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: | ≥95% (SDS-PAGE) |
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| Purity Detail: | Purified by multi-step chromatography. |
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| Activity: | Preincubation of MMP-20 catalytic domain at 0.4nM with the broad-spectrum inhibitor GM6001 (Prod. No. BML-EI300) at 0.1nM for 1 hour completely inhibits enzymatic activity. |
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| Specific Activity: | ≥ 10000pmol/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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| Scientific Background: | MMP-20 functions in tooth development and is implicated in cancer and oral pathology. |
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| Regulatory Status: | RUO - Research Use Only |
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General Literature References
Functions of KLK4 and MMP-20 in dental enamel formation: Y. Lu, et al.; Biol. Chem.
389, 695 (2008),
Abstract;
Expression and regulation of MMP-20 in human tongue carcinoma cells: A. Vaananen, et al.; J. Dent. Res.
80, 1884 (2001),
Abstract;
Immunohistochemical detection and distribution of enamelysin (MMP-20) in human odontogenic tumors: T. Takata, et al.; J. Dent. Res.
79, 1608 (2000),
Abstract;
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