Overview

  • Product name

    Recombinant Human ADAM21 protein
  • Protein length

    Protein fragment

Description

  • Nature

    Recombinant
  • Source

    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species

      Human
    • Molecular weight

      23 kDa
    • Amino acids

      200 to 400

Specifications

Our Abpromise guarantee covers the use of ab127086 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

  • Form

    Lyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20ºC.

    Constituents: 0.32% Tris HCl, 0.58% Sodium chloride

  • Reconstitution
    Reconstitute with water to desired concentration.

General Info

  • Alternative names

    • A disintegrin and metalloproteinase domain 21
    • ADA21_HUMAN
    • ADAM 21
    • ADAM metallopeptidase domain 21
    • ADAM metallopeptidase domain 21, preproprotein
    • Adam21
    • ADAM31
    • Disintegrin and metalloproteinase domain-containing protein 21
    see all
  • Function

    May be involved in sperm maturation and/or fertilization. May also be involved in epithelia functions associated with establishing and maintaining gradients of ions or nutrients.
  • Sequence similarities

    Contains 1 disintegrin domain.
    Contains 1 EGF-like domain.
    Contains 1 peptidase M12B domain.
  • Domain

    A tripeptide motif (VGE) within disintegrin-like domain could be involved in the binding to egg integrin receptor and thus could mediate sperm/egg binding.
    The cysteine-rich domain encodes putative cell-fusion peptides, which could be involved in sperm-egg fusion.
    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

    Has no obvious cleavage site for furin endopeptidase, suggesting that the proteolytic processing is regulated.
  • Cellular localization

    Membrane.
  • Information by UniProt

References

ab127086 has not yet been referenced specifically in any publications.

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