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MMP-8 proenzyme (human neutrophils)

ALX-200-421-C005 5 µg 157.00 USD
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Product Details

Alternative Name:Matrix metalloproteinase 8, Neutrophil collagenase, Collagenase-2
Source:Isolated from stimulated human neutrophil granulocytes (buffy coat). Requires activation.
UniProt ID:P22894
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.
Purity:≥90% (SDS-PAGE)
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.
Shipping:Dry Ice
Long Term Storage:-80°C
Use/Stability:Stable for 1 week when stored at +4°C and for serveral weeks when stored at -20°C.
Handling:Avoid freeze/thaw cycles.
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).
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.
Regulatory Status:RUO - Research Use Only

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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TIMP-1 (human neutrophils) 

Isolated from stimulated human neutrophils. The secreted protein consists of 184 amino acids, six disulfide bonds and two glycosylation sites containing N-linked oligosaccharides., ≥92% (SDS-PAGE, Western blot) | Print as PDF
ALX-200-426-C005 5 µg 372.00 USD
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