MMP8 (Cleaved-Leu101) rabbit pAb
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. 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. enzyme regulation: Cannot be activated without removal of the activation peptide. function: Can degrade fibrillar type I, II, and III collagens. similarity: Belongs to the peptidase M10A family. similarity: Contains 4 hemopexin-like domains. subcellular location: Stored in intracellular granules. tissue specificity: Neutrophils.
Product Specifications
Background
UniProt
P22894
Swiss Prot
P22894
Reactivity
Human; Mouse; Rat
Immunogen
Synthesized peptide derived from human MMP8 (Cleaved-Leu101)
Clonality
Polyclonal
Source
Rabbit
Applications
WB; IHC
Concentration
1 mg/ml
Dilution
WB 1:500-2000; IHC-p 1:50-300
Molecular Weight
40 53kD
Storage Conditions
-20°C/1 year
Observed Molecular Weight
40 53kD
Fragment
IgG
Subcellular Location
Cytoplasmic granule. Secreted, extracellular space, extracellular matrix . Stored in intracellular granules.
Other Product Names
Neutrophil collagenase (EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL)
Gene ID (Human)
4317
Available Sizes
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