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Rabbit anti-Human PDIA5 Polyclonal Antibody

The antibody against PDIA5 was raised in rabbit using the Human PDIA5 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB, IHC.

ADC-52415A

The antibody against PDIA5 was raised in rabbit using the Human PDIA5 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB, IHC.

$600.00

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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ADC-52415A ClonalityPolyclonal
Host SpeciesRabbitTarget NamePDIA5
Target SynonymsPdia5 antibody; PDIA5_HUMAN antibody; PDIR antibody; Protein disulfide isomerase related antibody; Protein disulfide isomerase-related protein antibody; Protein disulfide-isomerase A5 antibodyFormLiquid
Species ReactivityHuman, Mouse, RatIsotypeIgG
Storage Buffer50% Glycerol, Avoid freeze / thaw cycles., PBS with 0.02% sodium azidePurification MethodAntigen affinity purified
ConjugateNon-conjugatedApplicationELISA, IHC, WB
StorageUpon receipt

Immunogen Information


Immunogen DescriptionHuman PDIA5Target SpeciesHuman
Immunogen SequenceComplete sequences for the immunogen, target protein, and peptides are available upon request.Uniprot IDQ14554
Background Information
  • Uniprot Id

    Q14554

  • Target Species

    Human

  • Target Name

    PDIA5

  • Target Full Name

    Protein disulfide-isomerase A5

  • Target Subcellular Location

    Endoplasmic reticulum lumen.

  • Target Protein Families

    Protein disulfide isomerase family

  • Target Synonyms

    Pdia5; PDIA5_HUMAN; PDIR; Protein disulfide isomerase related; Protein disulfide isomerase-related protein; Protein disulfide-isomerase A5

  • Target Background

    This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, three catalytically active thioredoxin (TRX) domains, a TRX-like domain, and a C-terminal ER-retention sequence. The N-terminal TRX-like domain is the primary binding site for the major ER chaperone calreticulin and possibly other proteins and substrates as well. Alternative splicing results in multiple protein- and non-protein-coding transcript variants.

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