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Products:Signal Transduction >> Cytoskeleton / ECM >> Cell Adhesion >> Integrins >> Alpha
Overview
Product name
ADAM15 peptide (Propeptide domain)
See all ADAM15 products (3) ...
Protein description
Synthetic peptide ADAM15. (Note: the amino acid sequence is proprietary) This peptide was used as an immunogen for ab39160 - ADAM15 antibody - Propeptide domain.
Properties
Purity
>95% by SDS-PAGE
Form
Liquid
Storage instructions
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Storage buffer
Preservative: None
Constituents: 0.001% Tween 20, 30mM HEPES, 2mM EDTA, 150mM Sodium chloride, pH 6.75
Concentration
Concentration information loading...
Research areas
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
Signal Transduction >> Cytoskeleton / ECM >> Cell Adhesion >> Integrins >> Beta
Signal Transduction >> Cytoskeleton / ECM >> Cell Adhesion >> Integrins >> Alpha
Applications
Show applications key
Our Abpromise guarantee covers the use of ab41211 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
ELISA
WB
Application notes
ELISA: Use at an assay dependent dilution. WB: Use at an assay dependent dilution. This peptide can be used with studies using ab39160. Dilution optimised using Chromogenic detection. Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user.
Protein info
Function
Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain.
Tissue specificity
Expressed in colon and small intestine. Expressed in airway smooth muscle and glomerular mesangial cells (at protein level). Ubiquitously expressed. Overexpressed in atherosclerotic lesions. Constitutively expressed in cultured endothelium and smooth muscle. Expressed in chondrocytes. Expressed in airway smooth muscle and glomerular mesangial cells.
Sequence similarities
Contains 1 disintegrin domain.
Contains 1 EGF-like domain.
Contains 1 peptidase M12B domain.
Domain
The cytoplasmic domain interacts with endophilin I and sorting nexin 9.
Disintegrin domain binds to integrin alphaV-beta3.
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.
Post-translational
modifications
The precursor is cleaved by a furin endopeptidase.
Phosphorylation increases association with PTKs.
Cellular localization
Endomembrane system. Cell junction > adherens junction. Cell projection > cilium > flagellum. Cytoplasmic vesicle > secretory vesicle > acrosome. The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed.
Target information above from: UniProt accessionQ13444
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010).
References for ADAM15 peptide (Propeptide domain) (ab41211)
ab41211 has not yet been referenced specifically in any publications.
Publishing research using ab41211? Please let us know so that we can cite the reference in this datasheet
Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"