Overview

Description

  • NatureSynthetic
  • Amino Acid Sequence
    • Amino acids0 to 0

Specifications

Our Abpromise guarantee covers the use of ab41212 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    ELISA

    Western blot

  • Purity> 95 % by SDS-PAGE.

  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    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

General info

  • Alternative names
    • A disintegrin and metalloproteinase domain 15
    • A disintegrin and metalloproteinase domain 15
    • ADA15_HUMAN
    • ADAM 15
    • ADAM metallopeptidase domain 15
    • Adam15
    • and cysteine-rich protein 15
    • Disintegrin and metalloproteinase domain-containing protein 15
    • disintegrin-like
    • EC 3.4.24.
    • MDC 15
    • MDC-15
    • MDC15
    • Metalloprotease RGD disintegrin protein
    • Metalloproteinase like disintegrin like and cysteine rich protein 15
    • Metalloproteinase-like
    • Metargidin
    see all
  • FunctionActive 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 specificityExpressed 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 similaritiesContains 1 disintegrin domain.
    Contains 1 EGF-like domain.
    Contains 1 peptidase M12B domain.
  • DomainThe 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 localizationEndomembrane 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 accession Q13444 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

References for ADAM15 peptide (ab41212)

ab41212 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"