MMP19 (Cleaved-Tyr98) Rabbit Polyclonal Antibody

BT-AP03632-100ul

MMP19 (Cleaved-Tyr98) Rabbit Polyclonal Antibody

alternative products:Additional isoforms seem to exist|Catalytic activity:Cleaves aggrecan at the 360-Ser-|-Phe-361 site.|cofactor:Binds 1 zinc ion per subunit.|cofactor:Calcium.|disease:May play a role in pathological processes participating in rheumatoid arthritis (RA)-associated joint tissue destruction. Autoantigen anti-MMP19 are frequent in RA patients.|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:Strongly inhibited by TIMP-2| TIMP-3 and TIMP-4| while TIMP-1 is less efficient.|Endopeptidase that degrades various components of the extracellular matrix| such as aggrecan and cartilage oligomeric matrix protein (comp)| during development| haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis. Hydrolyzes collagen type IV| laminin| nidogen| nascin-C isoform| fibronectin| and type I gelatin.|PTM:Activated by autolytic cleavage after Lys-97.|Belongs to the peptidase M10A family.|Contains 4 hemopexin-like domains.|tissue specificity:Expressed in mammary gland| placenta| lung| pancreas| ovary| small intestine| spleen| thymus| prostate| testis colon| heart and blood vessel walls. Not detected in brain and peripheral blood leukocytes. Also expressed in the synovial fluid of normal and rheumatoid patients.|

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BT-AP03632-20ul

MMP19 (Cleaved-Tyr98) Rabbit Polyclonal Antibody

alternative products:Additional isoforms seem to exist|Catalytic activity:Cleaves aggrecan at the 360-Ser-|-Phe-361 site.|cofactor:Binds 1 zinc ion per subunit.|cofactor:Calcium.|disease:May play a role in pathological processes participating in rheumatoid arthritis (RA)-associated joint tissue destruction. Autoantigen anti-MMP19 are frequent in RA patients.|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:Strongly inhibited by TIMP-2| TIMP-3 and TIMP-4| while TIMP-1 is less efficient.|Endopeptidase that degrades various components of the extracellular matrix| such as aggrecan and cartilage oligomeric matrix protein (comp)| during development| haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis. Hydrolyzes collagen type IV| laminin| nidogen| nascin-C isoform| fibronectin| and type I gelatin.|PTM:Activated by autolytic cleavage after Lys-97.|Belongs to the peptidase M10A family.|Contains 4 hemopexin-like domains.|tissue specificity:Expressed in mammary gland| placenta| lung| pancreas| ovary| small intestine| spleen| thymus| prostate| testis colon| heart and blood vessel walls. Not detected in brain and peripheral blood leukocytes. Also expressed in the synovial fluid of normal and rheumatoid patients.|

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BT-AP03632-50ul

MMP19 (Cleaved-Tyr98) Rabbit Polyclonal Antibody

alternative products:Additional isoforms seem to exist|Catalytic activity:Cleaves aggrecan at the 360-Ser-|-Phe-361 site.|cofactor:Binds 1 zinc ion per subunit.|cofactor:Calcium.|disease:May play a role in pathological processes participating in rheumatoid arthritis (RA)-associated joint tissue destruction. Autoantigen anti-MMP19 are frequent in RA patients.|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:Strongly inhibited by TIMP-2| TIMP-3 and TIMP-4| while TIMP-1 is less efficient.|Endopeptidase that degrades various components of the extracellular matrix| such as aggrecan and cartilage oligomeric matrix protein (comp)| during development| haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis. Hydrolyzes collagen type IV| laminin| nidogen| nascin-C isoform| fibronectin| and type I gelatin.|PTM:Activated by autolytic cleavage after Lys-97.|Belongs to the peptidase M10A family.|Contains 4 hemopexin-like domains.|tissue specificity:Expressed in mammary gland| placenta| lung| pancreas| ovary| small intestine| spleen| thymus| prostate| testis colon| heart and blood vessel walls. Not detected in brain and peripheral blood leukocytes. Also expressed in the synovial fluid of normal and rheumatoid patients.|

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JOT-AP11343-50ul

MMP9 (Cleaved-Met94) Rabbit Polyclonal Antibody

366 €

BT-AP11342-100ul

MMP8 (Cleaved-Leu101) Rabbit Polyclonal Antibody

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.|

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BT-AP11342-20ul

MMP8 (Cleaved-Leu101) Rabbit Polyclonal Antibody

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.|

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