MMP1 (Cleaved-Ile271) Rabbit Polyclonal Antibody
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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.|
Fully tested in-house by ABMIUM, or supported by an advanced validation report from a partner reviewed by ABMIUM. Highest confidence. Non-conformities fully supported under the ABMIUM Product Promise.
Quality verified. Independent collaborator or expected-performance data available. Product meets ABMIUM quality standards.
Expected to work based on structural and biochemical data. Not yet directly tested by ABMIUM or a collaborator. No non-conformity support for this combination.
Not recommended for this application or species/sample combination. This may indicate either evidence of unsuitability or that the combination has not been tested and therefore cannot currently be recommended.
Evidence status by application and model.
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This product is manufactured by BT LAB and sold through ABMIUM without relabelling.
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Yes. Send your target, sample, application and experimental conditions through ABMIUM MATCH or technical support.
Unless the listing expressly states otherwise, ABMIUM products are supplied for research use only and are not for diagnostic or therapeutic use.
Matrix metallopeptidase 1 (MMP1), also known as interstitial collagenase or collagenase-1, is a secreted zinc-dependent matrix metalloproteinase involved in extracellular-matrix turnover. ABMIUM catalogue products linked below support research on MMP1 biology.
Biological function: Matrix metallopeptidase 1 (MMP1/interstitial collagenase) is a secreted zinc-dependent endopeptidase that cleaves fibrillar collagens and other extracellular-matrix substrates. By contributing to collagen breakdown and matrix remodelling, MMP1 participates in normal tissue turnover and is widely studied in repair, inflammation, fibrosis and tumour-stroma biology.
