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Recombinant Human Myomesin-2 (MYOM2), Truncated

ACP22793

Number
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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ACP22793 Target NameMYOM2
FormLyophilized powderExpression SystemCustom Production. Please inquire and provide the desire expression system.
Protein LengthPartialPurity>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 IDP54296
Background Information
  • Uniprot Id

    P54296

  • Target Species

    Human

  • Target Name

    MYOM2

  • Target Full Name

    Myomesin-2

  • Target Function

    Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent.

  • Target Subcellular Location

    Cytoplasm, myofibril, sarcomere, M line.

  • Target Synonyms

    165 kDa connectin associated protein; 165 kDa connectin-associated protein; 165 kDa titin associated protein; 165 kDa titin-associated protein; M band protein; M protein; M-protein; MYOM 2; MYOM2; MYOM2_HUMAN; Myomesin (M protein) 2 (165kD); Myomesin (M protein) 2 165kDa; Myomesin (M protein) 2; Myomesin 2; Myomesin family member 2; Myomesin-2; Titin associated protein 165 kD; Titin associated protein; TTNAP

  • Target Background

    The giant protein titin, together with its associated proteins, interconnects the major structure of sarcomeres, the M bands and Z discs. The C-terminal end of the titin string extends into the M line, where it binds tightly to M-band constituents of apparent molecular masses of 190 kD and 165 kD. The predicted MYOM2 protein contains 1, 465 amino acids. Like MYOM1, MYOM2 has a unique N-terminal domain followed by 12 repeat domains with strong homology to either fibronectin type III or immunoglobulin C2 domains. Protein sequence comparisons suggested that the MYOM2 protein and bovine M protein are identical.

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