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Rabbit anti-Human POLE4 Polyclonal Antibody

The antibody against POLE4 was raised in rabbit using the Recombinant Human DNA polymerase epsilon subunit 4 protein (8-117AA) 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.

ADC-03778A

The antibody against POLE4 was raised in rabbit using the Recombinant Human DNA polymerase epsilon subunit 4 protein (8-117AA) 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.

$299.00

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Specifications


Cat.No ADC-03778A ClonalityPolyclonal
Host SpeciesRabbitTarget NamePOLE4
FormLiquidSpecies ReactivityHuman
IsotypeIgGStorage Buffer0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4
Purification Method>95%, Protein G purifiedConjugateNon-conjugated
ApplicationELISA, IHCStorageUpon receipt

Immunogen Information


Immunogen DescriptionRecombinant Human DNA polymerase epsilon subunit 4 protein (8-117AA)Target SpeciesHuman
Immunogen SequenceComplete sequences for the immunogen, target protein, and peptides are available upon request.Uniprot IDQ9NR33
Background Information
  • Uniprot Id

    Q9NR33

  • Target Species

    Human

  • Target Name

    POLE4

  • Target Full Name

    DNA polymerase epsilon subunit 4

  • Target Function

    Accessory component of the DNA polymerase epsilon complex. Participates in DNA repair and in chromosomal DNA replication.

  • Target Subcellular Location

    Nucleus.

  • Target Synonyms

    DNA polymerase epsilon 4 accessory subunit; DNA polymerase epsilon p12 subunit; DNA polymerase epsilon subunit 4; DNA polymerase epsilon subunit p12; DNA polymerase II subunit 4; DPOE4_HUMAN; p12; POLE4; Polymerase (DNA directed) epsilon 4 (p12 subunit); Polymerase (DNA directed) epsilon 4; YHHQ1

  • Target Background

    POLE4 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexes for DNA transcription, replication, and packaging.[supplied by OMIM, Apr 2004]

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