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Rabbit anti-Human MPO Polyclonal Antibody

The antibody against MPO was raised in rabbit using the Recombinant Human Myeloperoxidase protein (165-278AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, IHC, IF.

ADC-50250A

The antibody against MPO was raised in rabbit using the Recombinant Human Myeloperoxidase protein (165-278AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, IHC, IF.

$299.00

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Specifications


Cat.No ADC-50250A ClonalityPolyclonal
Host SpeciesRabbitTarget NameMPO
FormLiquidSpecies ReactivityHuman
IsotypeIgGStorage Buffer0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4
Purification Method>95%, Protein G purifiedConjugateNon-conjugated
ApplicationELISA, IF, IHCStorageUpon receipt

Immunogen Information


Immunogen DescriptionRecombinant Human Myeloperoxidase protein (165-278AA)Target SpeciesHuman
Immunogen SequenceComplete sequences for the immunogen, target protein, and peptides are available upon request.Uniprot IDP05164
Background Information
  • Uniprot Id

    P05164

  • Target Species

    Human

  • Target Name

    MPO

  • Target Full Name

    Myeloperoxidase

  • Target Function

    Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity.

  • Target Involvement

    Myeloperoxidase deficiency (MPOD)

  • Target Subcellular Location

    Lysosome.

  • Target Protein Families

    Peroxidase family, XPO subfamily

  • Target Synonyms

    MPO; Myeloperoxidase (MPO)

  • Target 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.

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