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Recombinant Human Granzyme K (GZMK)

ACP00552

Number
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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ACP00552 Target NameGZMK
Target SynonymsFragmentin-3;Granzyme-3;NK-tryptase-2;NK-Tryp-2FormLiquid or Lyophilized powder
Expression SystemE.coliExpression Range27-264aa
Mol Weight32.8 kDaProtein LengthFull Length of Mature Protein
PurityGreater than 90% as determined by 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 IDP49863
Background Information
  • Uniprot Id

    P49863

  • Target Species

    Human

  • Target Name

    GZMK

  • Target Full Name

    Granzyme K

  • Target Subcellular Location

    Secreted. Cytoplasmic granule.

  • Target Protein Families

    Peptidase S1 family, Granzyme subfamily

  • Target Tissue Specificity

    Expressed in lung, spleen, thymus and peripheral blood leukocytes.

  • Target Research Area

    Cell Biology

  • Target Synonyms

    Fragmentin 3; Fragmentin-3; Fragmentin3; GRAK_HUMAN; Granzyme 3; granzyme K (granzyme 3; tryptase II); granzyme K (serine protease; granzyme 3; tryptase II); Granzyme K; Granzyme K precursor; Granzyme-3; Granzyme3; GranzymeK; GZMK; NK TRYP 2; NK TRYP2; NK tryptase 2; NK-TRYP-2; NK-tryptase-2; NKTRYP2; Serine protease granzyme 3; TRYP 2; TRYP2; Tryptase II; TryptaseII

  • Target Background

    This gene product is a member of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes (CTL) and natural killer (NK) cells share the remarkable ability to recognize, bind, and lyse specific target cells. They are thought to protect their host by lysing cells bearing on their surface 'nonself' antigens, usually peptides or proteins resulting from infection by intracellular pathogens. The protein described here lacks consensus sequences for N-glycosylation present in other granzymes.

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