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MMP-20 (catalytic domain) (human), (recombinant)

BML-SE540-0010 10 µg 506.00 USD
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Product Details

Alternative Name:Matrix metalloproteinase 20, Enamelysin
MW:19.9 kDa
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.
UniProt ID:O60882
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-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.
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.
Application Notes:Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors.
Shipping:Dry Ice
Long Term Storage:-80°C
Scientific Background:MMP-20 functions in tooth development and is implicated in cancer and oral pathology.
Regulatory Status:RUO - Research Use Only

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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