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Rabbit anti-Human CHDH Polyclonal Antibody

The antibody against CHDH was raised in rabbit using the Recombinant Human Choline dehydrogenase, mitochondrial protein (30-223AA) 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-09039A

The antibody against CHDH was raised in rabbit using the Recombinant Human Choline dehydrogenase, mitochondrial protein (30-223AA) 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-09039A ClonalityPolyclonal
Host SpeciesRabbitTarget NameCHDH
Target SynonymsCDH antibody; CHD antibody; CHDH antibody; CHDH_HUMAN antibody; Choline dehydrogenase antibody; mitochondrial antibodyFormLiquid
Species ReactivityHumanIsotypeIgG
Storage Buffer0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4Purification Method>95%, Protein G purified
ConjugateNon-conjugatedApplicationELISA, IHC
StorageUpon receipt

Immunogen Information


Immunogen DescriptionRecombinant Human Choline dehydrogenase, mitochondrial protein (30-223AA)Target SpeciesHuman
Immunogen SequenceComplete sequences for the immunogen, target protein, and peptides are available upon request.Uniprot IDQ8NE62
Background Information
  • Uniprot Id

    Q8NE62

  • Target Species

    Human

  • Target Name

    CHDH

  • Target Full Name

    Choline dehydrogenase, mitochondrial

  • Target Subcellular Location

    Mitochondrion inner membrane.

  • Target Protein Families

    GMC oxidoreductase family

  • Target Synonyms

    CDH; CHD; CHDH; CHDH_HUMAN; Choline dehydrogenase; mitochondrial

  • Target Background

    The protein encoded by this gene is a choline dehydrogenase that localizes to the mitochondrion. Variations in this gene can affect susceptibility to choline deficiency. A few transcript variants have been found for this gene, but the full-length nature of only one has been characterized to date.

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