Background:

Catalytic activity:Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I| II| IV| V. Cleaves gelatin chain alpha-2(I) > alpha-1(I).|cofactor:Binds 2 calcium ions per subunit.|cofactor:Binds 2 zinc 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.|Degrades casein| gelatins of types I| III| IV| and V| and fibronectin. Activates procollagenase.|Belongs to the peptidase M10A family.|

Classification:

Primary antibody

Alternative names:

MMP7 ;Cleaved-Tyr95; Matrilysin; EC 3.4.24.23; Matrin; Matrix metalloproteinase-7; MMP-7; Pump-1 protease; Uterine metalloproteinase

Species reactivity:

Human, Mouse, Rat

Host:

Rabbit

Isotype:

IgG

Immunogen:

Synthesized peptide derived from human MMP7 (Cleaved-Tyr95)

Concentration:

1 mg/ml

Molecular weight:

29370

Applications:

WB, ELISA

Storage:

-20°C for 1 year

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