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Anti-Phospho-PKR (Thr451) Rabbit Antibody [C9J9]

Catalog No.: F2372

Application: Reactivity: Human, Pig

Usage Information

Dilution
WB1:2000

Application
WB

Reactivity
Human, Pig

Source
Rabbit

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
62 kDa 68 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Datasheet & SDS

Biological Description

Specificity
Anti-Phospho-PKR (Thr451) Rabbit Antibody [C9J9] detects endogenous levels of PKR protein only when phosphorylated at Thr451.

Clone
C9J9

Synonym(s)
PKR, PRKR, EIF2AK2, 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, eIF-2A protein kinase 2, Protein kinase R

Background
Protein kinase R (PKR) is an interferon-induced serine/threonine kinase that plays a central role in innate antiviral defense and regulation of cell growth. Structurally, PKR contains two tandem dsRNA-binding motifs at its N-terminus, a flexible linker, and a C-terminal kinase domain that adopts a bilobal fold. PKR expression is upregulated by interferons and it becomes activated upon binding viral dsRNA, which promotes dimerization and autophosphorylation. Among several phosphorylation sites, threonine 451 (Thr451) in the activation loop is critical for enzymatic activity, as mutation of this residue impairs PKR function. Phosphorylation at Thr451, together with Thr446, stabilizes the active conformation, enhances dimerization, and enables PKR to phosphorylate eIF2α at serine 51, thereby blocking translation initiation and suppressing viral replication. Thus, PKR phosphorylation, particularly at Thr451, is essential for its role in antiviral immunity and tumor suppressor functions.

Background

Protein kinase R (PKR) is an interferon-induced serine/threonine kinase that plays a central role in innate antiviral defense and regulation of cell growth. Structurally, PKR contains two tandem dsRNA-binding motifs at its N-terminus, a flexible linker, and a C-terminal kinase domain that adopts a bilobal fold. PKR expression is upregulated by interferons and it becomes activated upon binding viral dsRNA, which promotes dimerization and autophosphorylation. Among several phosphorylation sites, threonine 451 (Thr451) in the activation loop is critical for enzymatic activity, as mutation of this residue impairs PKR function. Phosphorylation at Thr451, together with Thr446, stabilizes the active conformation, enhances dimerization, and enables PKR to phosphorylate eIF2α at serine 51, thereby blocking translation initiation and suppressing viral replication. Thus, PKR phosphorylation, particularly at Thr451, is essential for its role in antiviral immunity and tumor suppressor functions.

References
https://pubmed.ncbi.nlm.nih.gov/20088595/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

Tel: +1-832-582-8158 Ext:3
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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%