Phospho-PKR (T446) Recombinant Rabbit monoclonal Antibody IgG

SKU: BA111462-100µl

Fig1: Western blot analysis of Phospho-PKR(T446) on different lysates using anti-Phospho-PKR(T446) antibody at 1/1,000 dilution.

Positive control: 

  Lane 1: Hela treated with Calyculin A and TNF-alpha whole cell lysates 

  Lane 2: Untreated Hela whole cell lysates

Fig2: Immunohistochemical analysis of paraffin-embedded human kidney tissue using anti-Phospho-PKR(T446) antibody. Counter stained with hematoxylin.


Bon Opus Cat. #BA111462
  • Host Species; Species Reactivity

    Rabbit; Human
  • Immunogen

    Synthetic phospho-Peptide corresponding to residues surrounding Thr446 of human PKR.
  • Application Summary

  • Purification; Formulation

    ProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
  • ALTnames

    Interferon-induced, double-stranded RNA-activated protein kinase, Eukaryotic translation initiation factor 2-alpha kinase 2, Interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, Protein kinase RNA-activated, Tyrosine-protein kinase EIF2AK2, p68 kinase
  • Background

    An interferon-inducible, RNA-dependent protein serine/threonine kinase, PKR has various designations. Mouse PKR is known as DAI, dsJ, PI kinase, p65, p67 or TIK, whereas human PKR is known as p68 or p69. PKR phosphorylates its substrate, a subunit of protein synthesis initiation factor eIF-2 on Ser 51 to inhibit translation. PKR contains two dsRNA binding motifs required for its activation by dsRNA. Three kinds of regulation of PKR enzymatic activity occur, and these include transcriptional regulation in response to interferon, an autoregulatory mechanism controlling PKR expression at the level of translation, and posttranslational regulation by RNA mediated autophosphorylation. Human PKR contains at least 15 autophosphorylation sites, but only Thr-446 and Thr-451 in the activation loop are critical for its kinase activity. Thr-446 is the in vivo autophosphorylation site of PKR. Mutation of threonine to alanine at position 446 substantially reduces PKR function, and mutant kinase containing Ala-451 is completely inactive.(ET1607-20)

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