Product Details
Alternative Name: | Matrix metalloproteinase 8, Neutrophil collagenase, Collagenase-2 |
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MW: | ~85kDa. |
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Source: | Isolated from stimulated human neutrophil granulocytes (buffy coat). Requires activation. |
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EC: | 3.4.24.34 |
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UniProt ID: | P22894 |
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Concentration: | 100µg/ml |
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Formulation: | Liquid. In 50mM TRIS-HCl, pH 7.0, containing 200mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ 35, and 0.05% sodium azide. |
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Purity: | ≥90% (SDS-PAGE) |
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Specific Activity: | ≥60mU/mg protein (Y. Masui, et al.; Biochem. Med. 17, 215 (1977)). One unit is defined as the amount of enzyme that hydrolyzes 1µmol 2,4-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0. |
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Shipping: | Shipped on Dry Ice |
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Long Term Storage: | -80°C |
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Use/Stability: | Stable for 1 week when stored at +4°C and for serveral weeks when stored at -20°C. |
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Handling: | Avoid freeze/thaw cycles. |
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Scientific Background: | MMP-8 is a glycoprotein containing complex N-linked oligosaccharides. It hydrolyzes type I over type II, and III collagens. Activated MMP-8 is inhibited by TIMP-1 (Prod. No. ALX-200-426). |
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Technical Info/Product Notes: | Precursor enzyme needs activation using 2mM AMPA (aminophenylmercuric acetate) or 1mM mersalylic acid for 60 min. at 37°C. Alternatively use 0.1mM PCMB (p-chloromercuribenzoate) or 10µg/ml trypsin for 20 min. at 25°C; PCMB is substantially more effective. |
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Regulatory Status: | RUO - Research Use Only |
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Product Literature References
A novel role for matrix metalloproteinase-8 in sepsis: P.D. Solan, et al.; Crit. Care Med.
40, 379 (2012),
Abstract;
Full Text
A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases: C.G. Knight, et al.; FEBS Lett.
296, 263 (1992),
Abstract;
Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase: S.K. Mallya, et al.; Biochemistry
29, 10628 (1990),
Abstract;
Secreted forms of human neutrophil collagenase: K.A. Hasty, et al.; J. Biol. Chem.
261, 5645 (1986),
Abstract;
Full Text
Synthetic substrates for vertebrate collagenase: Y. Masui, et al.; Biochem. Med.
17, 215 (1977),
Abstract;
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