Render Target: STATIC
Render Timestamp: 2024-12-26T11:10:53.794Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-04-05 20:22:47.510
Product last modified at: 2024-06-27T13:36:08.992Z
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PDP - Template Name: Blocking Peptide
PDP - Template ID: *******6db2f4c

Phospho-eIF2α (Ser51) Blocking Peptide #1221

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Important Ordering Details

Custom Ordering Details: This product is assembled upon order. Please allow two-four weeks for your product to be processed.

    Product Information

    Product Usage Information

    Use as a blocking reagent to evaluate the specificity of antibody reactivity in western blotting and dot blot protocols. For western blotting, add an equal volume of peptide as volume of antibody used in 10 ml total volume, and incubate at room temperature for 30 minutes before allowing to react with the blot. Recommended antibody dilution can be found on the Phospho-eIF2alpha (Ser51) (119A11) Rabbit mAb #3597 datasheet.

    Storage

    Supplied in 20 mM potassium phosphate (pH 7.0), 50 mM NaCl, 0.1 mM EDTA, 1 mg/ml BSA and 5% glycerol. 1% DMSO. Store at –20°C.

    Product Description

    This peptide is used to block Phospho-eIF2alpha (Ser51) (119A11) Rabbit mAb (#3597) and Phospho-eIF2α (Ser51) (D9G8) XP® Rabbit mAb (#3398). Human eIF2alpha residue Ser52 historically has been referenced as Ser51.

    Quality Control

    The quality of the peptide was evaluated by reverse-phase HPLC and by mass spectrometry. The peptide blocks Phospho-eIF2alpha (Ser51) (119A11) Rabbit mAb #3597 signal in both dot blot and western blotting.

    Background

    Phosphorylation of the eukaryotic initiation factor 2 (eIF2) α subunit is a well-documented mechanism to downregulate protein synthesis under a variety of stress conditions. eIF2 binds GTP and Met-tRNAi and transfers Met-tRNA to the 40S subunit to form the 43S preinitiation complex (1,2). eIF2 promotes a new round of translation initiation by exchanging GDP for GTP, a reaction catalyzed by eIF2B (1,2). Kinases that are activated by viral infection (PKR), endoplasmic reticulum stress (PERK/PEK), amino acid deprivation (GCN2), or heme deficiency (HRI) can phosphorylate the α subunit of eIF2 (3,4). This phosphorylation stabilizes the eIF2-GDP-eIF2B complex and inhibits the turnover of eIF2B. Induction of PKR by IFN-γ and TNF-α induces potent phosphorylation of eIF2α at Ser51 (5,6).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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