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Description :Rabbit Polyclonal Antibody
Specificity :Recognizes the EIF2AK2 protein
Cited Applications :WB, ELISA, IF, IHC
Cross Reactivity :Human, Mouse and Rat
Host / Isotype / Clone# :Rabbit, IgG
Immunogen :EIF2AK2 antibody was raised against a peptide corresponding to 14 amino acids near the carboxy terminus of human EIF2AK2
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 EIF2AK2 in A431 whole cell lysate with EIF2AK2 antibody at (A) 0.5, (B) 1 and (C) 2 ug/ml.
Sample Data :Immunohistochemistry of EIF2AK2 in rat lung tissue with EIF2AK2 antibody at 2.5 ug/ml.
Scientific Background :EIF2AK2 (also known as double-stranded RNA-activated protein kinase) is a protein kinase that has been shown to be involved in HIV/gp120-associated neurodegeneration (1). EIF2AK2 acts as a critical mediator of gp120 neurotoxicity and is a substrate for a family of protein kinases that respond to various forms of environmental stress. Activation of EIF2AK2 leads to its autophosphorylation and then phosphorylation of its natural substrate, the alpha subunit of eukaryotic protein synthesis initiation factor-2. EIF2AK2 plays a critical role in mRNA translation, cell proliferation and apoptosis. A novel cross-talk between the EIF2AKs and p53 has been shown that has implications in cell proliferation and tumorigenesis (2).
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