MMP7 (Cleaved-Tyr95) rabbit pAb
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MMP7 (Cleaved-Tyr95) rabbit pAb
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., domain: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., function:Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase., similarity:Belongs to the peptidase M10A family.Description :
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. Domain: 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. function: Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase. similarity: Belongs to the peptidase M10A family.UniProt :
P09237Swiss Prot :
P09237Reactivity :
Human; Mouse; RatImmunogen :
Synthesized peptide derived from human MMP7 (Cleaved-Tyr95)Clonality :
PolyclonalSource :
RabbitApplications :
WB; ELISA; IHCConcentration :
1 mg/mlDilution :
WB 1:500-2000; IHC-p 1:50-300; ELISA 2000-20000Molecular Weight :
19 29kDStorage Conditions :
-20°C/1 yearObserved Molecular Weight :
19 29kDFragment :
IgGSubcellular Location :
Secreted, extracellular space, extracellular matrix .Other Product Names :
Matrilysin (EC 3.4.24.23; Matrin; Matrix metalloproteinase-7; MMP-7; Pump-1 protease; Uterine metalloproteinase)Gene ID (Human) :
4316

