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Recombinant Human Annexin A9 (ANXA9)

ACP20863

Number
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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ACP20863 Target NameANXA9
Target Synonymsannexin 31; annexin 31; formerly; Annexin A9; Annexin XXXI; Annexin-31; Annexin-9; ANX31; ANX31; formerly; ANXA9; ANXA9_HUMAN; PemphaxinFormLyophilized powder
Expression SystemCustom Production. Please inquire and provide the desire expression system.Expression Range1-345
Protein LengthFull length proteinPurity>85% (SDS-PAGE)
Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDO76027
Background Information
  • Uniprot Id

    O76027

  • Target Species

    Human

  • Target Name

    ANXA9

  • Target Full Name

    Annexin A9

  • Target Function

    Low affinity receptor for acetylcholine known to be targeted by disease-causing pemphigus vulgaris antibodies in keratinocytes.

  • Target Protein Families

    Annexin family

  • Target Tissue Specificity

    Expressed in the stratified squamous skin epithelium, but not in epithelia of other types (at protein level).

  • Target Research Area

    Signal Transduction

  • Target Synonyms

    annexin 31; annexin 31; formerly; Annexin A9; Annexin XXXI; Annexin-31; Annexin-9; ANX31; ANX31; formerly; ANXA9; ANXA9_HUMAN; Pemphaxin

  • Target Background

    The annexins are a family of calcium-dependent phospholipid-binding proteins. Members of the annexin family contain 4 internal repeat domains, each of which includes a type II calcium-binding site. The calcium-binding sites are required for annexins to aggregate and cooperatively bind anionic phospholipids and extracellular matrix proteins. This gene encodes a divergent member of the annexin protein family in which all four homologous type II calcium-binding sites in the conserved tetrad core contain amino acid substitutions that ablate their function. However, structural analysis suggests that the conserved putative ion channel formed by the tetrad core is intact.

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