Anti-phospho-EIF2AK2 (Thr446)(P80-65R)

Anti-phospho-EIF2AK2 (Thr446)(P80-65R)

  • $270.00


Description :Rabbit Polyclonal Antibody

Species :

Tag :

Expression System:

Sequence :

Specificity :Recognizes the EIF2AK2 protein phosphorylated at threonine 446

Cited Applications :WB, IHC

Cross Reactivity :Human and Mouse

Host / Isotype / Clone# :Rabbit, IgG

Immunogen :Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr446

Purification :Affinity chromatography

Stability :Store at 4oC (add 0.1% NaN3) for several months, and at -20oC for longer periods. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

Sample Data :Western blot analysis of extracts from K562 cells using EIF2AK2 antibody (lanes 1 and 2) and anti-phospho-EIF2AK2 (Thr446) antibody (lanes 3 and 4).

Scientific Background :EIF2AK2 (also known as double-stranded RNA-activated protein kinase and PKR) is a protein kinase that is involved in HIV/gp120-associated neurodegeneration (1). EIF2AK2 is a mediator of gp120 neurotoxicity and is a substrate for a family of protein kinases involved in environmental stress responses. Activation of EIF2AK2 by dsRNA leads to autophosphorylation at Thr446/451. Activated EIF2AK2 phosphorylates the alpha subunit of EIF2, which in turn inhibits protein synthesis. EIF2AK2 plays a critical role in mRNA translation, cell proliferation and apoptosis. Crosstalk between EIF2AKs and p53 has implications in cell proliferation and tumorigenesis (2).

References :
1. Baltzis, D. et al: The eIF2alpha kinases PERK and PKR activate glycogen synthase kinase 3 to promote the proteasomal degradation of p53. J. Biol Chem. 2007; 282(43):31675-87

2. Alirezaei, M. et al: Human immunodeficiency virus-1/surface glycoprotein 120 induces apoptosis through RNA-activated protein kinase signaling in neurons. J. Neurosci. 2007;27(41):11047-55.

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Research Areas :Angiogenesis, Cellular Stress, Inflammation, Neurobiology, Ser/Thr Kinases, Neurobiology, Inflammation, Cellular Stress, Angiogenesis, Ser/Thr Kinases