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Read our guarantee »Products:Cardiovascular >> Angiogenesis >> Adhesion / ECM >> Matrix Metalloproteinases >> MMP
MMP1 peptide (Carboxyterminal end)
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Synthetic peptide MMP1. (Note: the amino acid sequence is proprietary) This peptide was used as an immunogen for ab38926 - MMP1 antibody - Carboxyterminal end.
>95% by SDS-PAGE
Liquid
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Preservative: None
Constituents: 0.001% Tween 20, 30mM HEPES, 2mM EDTA, 150mM Sodium chloride
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Cardiovascular >> Atherosclerosis >> Thrombosis >> Endothelial mediators/regulators
Cancer >> Tumor biomarkers >> Enzymes >> MMPs
Cell Biology >> Proteolysis / Ubiquitin >> Proteolytic enzymes >> Metalloprotease >> MMPs
Cancer >> Invasion/microenvironment >> Angiogenesis >> ECM enzymes >> MMPs
Signal Transduction >> Cytoskeleton / ECM >> Extracellular Matrix >> ECM Enzymes >> MMP
Cardiovascular >> Angiogenesis >> Adhesion / ECM >> Matrix Metalloproteinases >> MMP
Our Abpromise guarantee covers the use of ab41017 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
ELISA: Use at an assay dependent dilution. WB: Use at an assay dependent dilution. This peptide can be used with studies using ab38926. Dilution optimised using Chromogenic detection. Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user.
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.
Belongs to the peptidase M10A family.
Contains 4 hemopexin-like domains.
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).
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.
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.
Secreted > extracellular space > extracellular matrix.
Target information above from: UniProt accessionP03956
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010).
ab41017 has not yet been referenced specifically in any publications.
Publishing research using ab41017? Please let us know so that we can cite the reference in this datasheet
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