MMP7 (Cleaved-Tyr95) rabbit pAb
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.
Product Specifications
Background
UniProt
P09237
Swiss Prot
P09237
Reactivity
Human; Mouse; Rat
Immunogen
Synthesized peptide derived from human MMP7 (Cleaved-Tyr95)
Clonality
Polyclonal
Source
Rabbit
Applications
WB; ELISA; IHC
Concentration
1 mg/ml
Dilution
WB 1:500-2000; IHC-p 1:50-300; ELISA 2000-20000
Molecular Weight
19 29kD
Storage Conditions
-20°C/1 year
Observed Molecular Weight
19 29kD
Fragment
IgG
Subcellular 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
Available Sizes
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