Overview

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Species
      Human
    • Amino acids
      208 to 738

Specifications

Our Abpromise guarantee covers the use of ab53659 in the following tested applications.

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

  • Applications

    SDS-PAGE

  • Purity
    > 95 % SDS-PAGE.

  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.

General Info

  • Alternative names
    • A disintegrin and metalloproteinase domain 12
    • ADA12_HUMAN
    • ADAM 12
    • ADAM metallopeptidase domain 12
    • ADAM12
    • CAR10
    • Disintegrin and metalloproteinase domain-containing protein 12
    • MCMP
    • MCMPMltna
    • Meltrin alpha
    • Meltrin-alpha
    • Metalloprotease disintegrin 12 transmembrane
    • MLTN
    • MLTNA
    • OTTHUMP00000046766
    see all
  • Function
    Involved 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 specificity
    Isoform 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 similarities
    Contains 1 disintegrin domain.
    Contains 1 EGF-like domain.
    Contains 1 peptidase M12B domain.
  • Domain
    The 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 localization
    Secreted and Cell membrane.
  • Information by UniProt

References

ab53659 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"

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