MPO rabbit pAb

CAT:
855-ES4081-01
Size:
50 µL
  • Availability: 24/48H Stock Items & 2 to 6 Weeks non Stock Items.
  • Dry Ice Shipment: No
MPO rabbit pAb - image 1

MPO rabbit pAb

  • Background :

    Myeloperoxidase (MPO) is a heme protein synthesized during myeloid differentiation that constitutes the major component of neutrophil azurophilic granules. Produced as a single chain precursor, myeloperoxidase is subsequently cleaved into a light and heavy chain. The mature myeloperoxidase is a tetramer composed of 2 light chains and 2 heavy chains. This enzyme produces hypohalous acids central to the microbicidal activity of neutrophils. [provided by RefSeq, Nov 2014]
  • Description :

    Myeloperoxidase (MPO) is a heme protein synthesized during myeloid differentiation that constitutes the major component of neutrophil azurophilic granules. Produced as a single chain precursor, myeloperoxidase is subsequently cleaved into a light and heavy chain. The mature myeloperoxidase is a tetramer composed of 2 light chains and 2 heavy chains. This enzyme produces hypohalous acids central to the microbicidal activity of neutrophils. [provided by RefSeq, Nov 2014],
  • Product Name Alternative :

    MPO; Myeloperoxidase; MPO
  • UniProt :

    P05164
  • Swiss Prot :

    P05164
  • Reactivity :

    Human; Mouse; Rat
  • Immunogen :

    The antiserum was produced against synthesized peptide derived from the N-terminal region of human MPO. AA range:41-90
  • Target :

    MPO
  • Clonality :

    Polyclonal
  • Source :

    Rabbit
  • Applications :

    WB; IHC; IF; ELISA
  • Concentration :

    1 mg/ml
  • Dilution :

    IHC-p: 100-300.Western Blot: 1/500 - 1/2000. ELISA: 1/20000. Not yet tested in other applications.
  • Buffer :

    -20°C/1 year
  • Molecular Weight :

    85kD
  • Storage Conditions :

    -20°C/1 year
  • Observed Molecular Weight :

    85kD
  • Fragment :

    IgG
  • Subcellular Location :

    Lysosome.
  • Other Product Names :

    MPO; Myeloperoxidase; MPO
  • Gene ID (Human) :

    4353

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