Background:

Catalytic activity:Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7| this enzyme cleaves type III collagen more slowly than type I.|cofactor:Binds 2 zinc ions per subunit.|cofactor:Binds 3 calcium ions per subunit.|The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion| thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.|enzyme regulation:Cannot be activated without removal of the activation peptide.|Can degrade fibrillar type I| II| and III collagens.|Belongs to the peptidase M10A family.|Contains 4 hemopexin-like domains.|subcellular location:Stored in intracellular granules.|tissue specificity:Neutrophils.|

Classification:

Primary antibody

Alternative names:

MMP8 ;Cleaved-Leu101; Neutrophil collagenase; EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL

Species reactivity:

Human, Mouse, Rat

Host:

Rabbit

Isotype:

IgG

Immunogen:

Synthesized peptide derived from human MMP8 (Cleaved-Leu101)

Concentration:

1 mg/ml

Molecular weight:

51370

Applications:

WB, ELISA

Storage:

-20°C for 1 year

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