|Calculated MW||40/42 kDa|
|Other Names||Neutrophil collagenase (EC 126.96.36.199) (Matrix metalloproteinase-8) (MMP-8) (PMNL collagenase) (PMNL-CL)|
|Source||Human neutrophil granulocytes (Buffy Coat)|
|Storage||-80°C; In 50 mM Tris-HCl, pH 7; 200 mM NaCl; 5 mM CaCl₂; 1 µM ZnCl₂; 0.05% Brij 35; 0,05% NaN₃|
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Provided below are standard protocols that you may find useful for product applications.
Human neutrophil collagenase (HNC) has been purified from extracts of fresh and outdated buffy coats and from exudates of phorbol myristate acetate-stimulated neutrophils. The MMP-8 present in the starting material can either be latent or active, or have an app. relative molecular mass of 75-kDa and/or 58-kDa. The rather complex pattern of activation of the latent 58-kDa and 75-kDa species by trypsin, organomercurials and oxidants has been investigated. MMP-8 was shown to preferentially hydrolyze type I over type II, and type III collagens in solution and to be a glycoprotein that contains complex N-linked oligosaccharides leading to multiple forms of MMP-8 in SDS-PAGE. The action of endoglycosidase on the latent 58-kDa form produces 42/40-kDa species (Gao et al. 1992, Mallya et al. 1990). This indicates that MMP-8 is an N-linked, complex glycoprotein that appears to be glycosylated at multiple sites.
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