• Product nameAnti-PKR antibody
    See all PKR primary antibodies
  • Description
    Rabbit polyclonal to PKR
  • SpecificityDetects endogenous levels of total PKR protein.
  • Tested applicationsSuitable for: WB, IHC-P, ELISAmore details
  • Species reactivity
    Reacts with: Human
  • Immunogen

    Synthetic non-phosphopeptide:


    , corresponding to amino acids 444-448 of Human PKR, from around the phosphorylation site of threonine 446.

  • Positive control
    • Human breast carcinoma tissue. K562 cells.


  • FormLiquid
  • Storage instructionsShipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
  • Storage bufferPreservative: 0.02% Sodium Azide
    Constituents: 50% Glycerol, PBS (without Mg2+ and Ca2+), 150mM Sodium chloride, pH 7.4
  • Concentration information loading...
  • PurityImmunogen affinity purified
  • Purification notesPurified from rabbit antiserum by affinity chromatography using epitope specific immunogen.
  • ClonalityPolyclonal
  • IsotypeIgG
  • Research areas


Our Abpromise guarantee covers the use of ab47509 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB 1/500 - 1/1000. Detects a band of approximately 62 kDa (predicted molecular weight: 62 kDa).
IHC-P Use at an assay dependent concentration.
ELISA 1/20000.


  • FunctionFollowing activation by double-stranded RNA in the presence of ATP, the kinase becomes autophosphorylated and can catalyze the phosphorylation of the translation initiation factor EIF2S1, which leads to an inhibition of the initiation of protein synthesis. Double-stranded RNA is generated during the course of a viral infection.
  • Sequence similaritiesBelongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.
    Contains 2 DRBM (double-stranded RNA-binding) domains.
    Contains 1 protein kinase domain.
  • Post-translational
    Autophosphorylated on several Ser and Thr residues. Autophosphorylation of Thr-451 is dependent on Thr-446 and is stimulated by dsRNA binding and dimerization. Autophosphorylation apparently leads to the activation of the kinase.
  • Information by UniProt
  • Database links
  • Alternative names
    • Double stranded RNA activated protein kinase; antibody
    • E2AK2_HUMAN antibody
    • eIF-2A protein kinase 2 antibody
    • EIF2AK1 antibody
    • EIF2AK2 antibody
    • Eukaryotic translation initiation factor 2 alpha kinase 2 antibody
    • Eukaryotic translation initiation factor 2-alpha kinase 2 antibody
    • HGNC:9437 antibody
    • Interferon induced double stranded RNA activated protein kinase antibody
    • Interferon inducible elF2 alpha kinase antibody
    • Interferon inducible RNA dependent protein kinase antibody
    • Interferon-induced, double-stranded RNA-activated protein kinase antibody
    • Interferon-inducible RNA-dependent protein kinase antibody
    • MGC126524 antibody
    • P1/eIF-2A protein kinase antibody
    • P1/eIF2A protein kinase antibody
    • p68 kinase antibody
    • PKR antibody
    • PPP1R83 antibody
    • PRKR antibody
    • Protein kinase interferon inducible double stranded RNA dependent antibody
    • Protein kinase RNA activated antibody
    • Protein kinase RNA-activated antibody
    • Protein phosphatase 1 regulatory subunit 83 antibody
    • Serine/threonine protein kinase TIK antibody
    • Tyrosine protein kinase EIF2AK2 antibody
    see all

Anti-PKR antibody images

  • ab47509, at 1/50 dilution, staining Human breast carcinoma by Immunohistochemistry, Paraffin embedded tissue. Left panel: no immunogenic peptide; right panel: immunogenic peptide added.
  • All lanes : Anti-PKR antibody (ab47509) at 1 µg/ml

    Lane 1 : K562 cells treated with starvation (24 hours)
    Lane 2 : K562 cells treated with starvation (24 hours) with blocking peptide

    Predicted band size : 62 kDa
    Observed band size : 62 kDa

References for Anti-PKR antibody (ab47509)

ab47509 has not yet been referenced specifically in any publications.

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