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Sigma-Aldrich

Anti-phospho-PKR (Thr446) Antibody

Upstate®, from rabbit

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human

manufacturer/tradename

Upstate®

technique(s)

western blot: suitable

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

phosphorylation (pThr446)

Gene Information

human ... EIF2AK2(5610)

Specificity

phospho-PKR

Immunogen

Peptide corresponding to amino acids surrounding Thr446 of human PKR.

Application

Anti-phospho-PKR (Thr446) Antibody is an antibody against phospho-PKR (Thr446) for use in WB.
Research Category
Signaling
Research Sub Category
Cytoskeletal Signaling

Quality

routinely evaluated by immunoblot in RIPA lysates from HeLa cells that had been stimulated with IFN alpha overnight followed by treatment with calyculin A for 15 minutes

Target description

68 kDa

Physical form

0.1M Tris-glycine, pH 7.4, 0.15M NaCl, 0.05% sodium azide before the addition of glycerol to 30%
Format: Purified
Protein A purified

Storage and Stability

2 years at -20°C

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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X Saelens et al.
The Journal of biological chemistry, 276(45), 41620-41628 (2001-09-14)
The protein kinase PKR is a major player in the cellular antiviral response, acting mainly by phosphorylation of the alpha-subunit of the eukaryotic translation initiation factor 2 (eIF2-alpha) to block de novo protein synthesis. PKR activation requires binding of double-stranded
Dario Paolo et al.
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Ka-Chun Suen et al.
The Journal of biological chemistry, 278(50), 49819-49827 (2003-09-17)
One of the hallmarks of Alzheimer's disease is extracellular accumulation of senile plaques composed primarily of aggregated beta-amyloid (Abeta) peptide. Treatment of cultured neurons with Abeta peptide induces neuronal death in which apoptosis is suggested to be one of the
Shien Hu et al.
Gastroenterology, 133(6), 1893-1904 (2007-12-07)
Inducible heat shock proteins (iHsp), Hsp25/27 and Hsp70, play essential roles in protecting cells against stress and, in intestinal mucosal inflammation, potentially lessening the extent and severity of injury. We examined the expression and regulation of iHsp in human and
Shuen-Ing Tschen et al.
Diabetes, 58(6), 1312-1320 (2009-02-21)
The aim of this study was to elucidate whether age plays a role in the expansion or regeneration of beta-cell mass. We analyzed the capacity of beta-cell expansion in 1.5- and 8-month-old mice in response to a high-fat diet, after

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