MMP1 (Cleaved-Ile271) Rabbit Polyclonal Antibody
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quantity
Produktdetaljer
Katalognummer: 772 - BT-AP03630-100ul
Produktkategori: Företag och industri > Vetenskap och laboratorium
Gentaur
Storlek: 100ul
Parameters
| Additional information | WB, ELISA |
|---|---|
| Storage and shipping | -20°C for 1 year |
BT-AP03630-100ul
MMP1 (Cleaved-Ile271) Rabbit Polyclonal Antibody
Catalytic activity:Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus| at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.|cofactor:Binds 2 zinc ions per subunit.|cofactor:Binds 4 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.|There are two distinct domains in this protein; the catalytic N-terminal| and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases).|enzyme regulation:Can be activated without removal of the activation peptide.|Cleaves collagens of types I| II| and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection| interacts and cleaves the secreted viral Tat protein| leading to a decrease in neuronal Tat's mediated neurotoxicity.|online information:Collagenase entry|PTM:Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.|Belongs to the peptidase M10A family.|Contains 4 hemopexin-like domains.|subunit:Interacts with HIV-1 Tat.|
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BT-AP03630-20ul
MMP1 (Cleaved-Ile271) Rabbit Polyclonal Antibody
Catalytic activity:Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus| at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.|cofactor:Binds 2 zinc ions per subunit.|cofactor:Binds 4 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.|There are two distinct domains in this protein; the catalytic N-terminal| and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases).|enzyme regulation:Can be activated without removal of the activation peptide.|Cleaves collagens of types I| II| and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection| interacts and cleaves the secreted viral Tat protein| leading to a decrease in neuronal Tat's mediated neurotoxicity.|online information:Collagenase entry|PTM:Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.|Belongs to the peptidase M10A family.|Contains 4 hemopexin-like domains.|subunit:Interacts with HIV-1 Tat.|
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BT-AP03630-50ul
MMP1 (Cleaved-Ile271) Rabbit Polyclonal Antibody
Catalytic activity:Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus| at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.|cofactor:Binds 2 zinc ions per subunit.|cofactor:Binds 4 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.|There are two distinct domains in this protein; the catalytic N-terminal| and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases).|enzyme regulation:Can be activated without removal of the activation peptide.|Cleaves collagens of types I| II| and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection| interacts and cleaves the secreted viral Tat protein| leading to a decrease in neuronal Tat's mediated neurotoxicity.|online information:Collagenase entry|PTM:Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.|Belongs to the peptidase M10A family.|Contains 4 hemopexin-like domains.|subunit:Interacts with HIV-1 Tat.|
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BT-AP11338-100ul
MMP13 (Cleaved-Tyr104) Rabbit Polyclonal Antibody
cofactor:Binds 2 zinc ions per subunit.|cofactor:Binds 4 calcium ions per subunit.|disease:Defects in MMP13 are the cause of spondyloepimetaphyseal dysplasia type 2 (SEMD2)
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BT-AP11338-20ul
MMP13 (Cleaved-Tyr104) Rabbit Polyclonal Antibody
cofactor:Binds 2 zinc ions per subunit.|cofactor:Binds 4 calcium ions per subunit.|disease:Defects in MMP13 are the cause of spondyloepimetaphyseal dysplasia type 2 (SEMD2)
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BT-AP11338-50ul
MMP13 (Cleaved-Tyr104) Rabbit Polyclonal Antibody
cofactor:Binds 2 zinc ions per subunit.|cofactor:Binds 4 calcium ions per subunit.|disease:Defects in MMP13 are the cause of spondyloepimetaphyseal dysplasia type 2 (SEMD2)
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