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ADAM10 peptide (Aminoterminal end)
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This peptide was used as an immunogen for ab39153 - ADAM10 antibody - Aminoterminal 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, pH 6.75
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Cell Biology >> Proteolysis / Ubiquitin >> Proteolytic enzymes >> Metalloprotease >> ADAMs
Cancer >> Invasion/microenvironment >> ECM >> Extracellular matrix >> ADAM protein family
Signal Transduction >> Cytoskeleton / ECM >> Extracellular Matrix >> ECM Enzymes >> ADAM Protein Family
Cell Biology >> Apoptosis >> Receptors >> Receptor Processing
Our Abpromise guarantee covers the use of ab41167 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 ab39153. Dilution optimised using Chromogenic detection. Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user.
Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-
-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis.
Expressed in spleen, lymph node, thymus, peripheral blood leukocyte, bone marrow, cartilage, chondrocytes and fetal liver.
Contains 1 disintegrin domain.
Contains 1 peptidase M12B 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.
The precursor is cleaved by a furin endopeptidase.
Cell membrane. Endomembrane system. Is localized in the plasma membrane but is predominantly expressed in the Golgi apparatus and in released membrane vesicles derived likely from the Golgi.
Target information above from: UniProt accessionO14672
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010).
ab41167 has not yet been referenced specifically in any publications.
Publishing research using ab41167? Please let us know so that we can cite the reference in this datasheet
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