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Overview

  • Product nameADAM12 peptide (2-15)See all ADAM12 proteins and peptides ...
  • Protein descriptionSynthetic peptide: AARPLPVSPARAL-C, corresponding to N terminal amino acids 2-15 of Human ADAM12. This peptide was used as an immunogen for ab28747 - ADAM12 antibody.

    • Properties

  • FormLiquid
  • Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
  • Concentration information loading...
  • SequenceAARPLPVSPARAL-C
  • Research Areas

    • Protein info

    • Alternative names
        A disintegrin and metalloproteinase domain 12A disintegrin and metalloproteinase domain 12ADA12_HUMAN
        ADAM 12ADAM metallopeptidase domain 12ADAM12Disintegrin and metalloproteinase domain-containing protein 12MCMPMCMPMltnaMCMPMltnaMeltrin alphaMeltrin-alphaMLTNMLTNAOTTHUMP00000046766
      see all
  • FunctionInvolved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors.
  • Tissue specificityIsoform 1 is expressed in placenta and skeletal, cardiac, and smooth muscle. Isoform 2 seems to be expressed only in placenta or in embryo and fetus. Both forms were expressed in some tumor cells lines. Not detected in brain, lung, liver, kidney or pancreas.
  • Sequence similaritiesContains 1 disintegrin domain.
    Contains 1 EGF-like domain.
    Contains 1 peptidase M12B domain.
  • DomainThe cysteine-rich domain supports cell adhesion through syndecans and triggers signaling events that lead to beta-1 integrin-dependent cell spreading. In carcinomas cells the binding of this domain to syndecans does not allow the integrin-mediated cell spreading.
    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.
  • Cellular localizationSecreted and Cell membrane.

    • Target information above from: UniProt accession O43184 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

    References for ADAM12 peptide (2-15) (ab45636)

    ab45636 has not yet been referenced specifically in any publications.

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