Render Target: STATIC
Render Timestamp: 2024-12-26T12:06:50.979Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-08-01 15:31:46.766
Product last modified at: 2024-12-17T22:15:13.695Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

Phospho-eIF2α (Ser51) (119A11) Rabbit mAb #3597

Filter:
  • WB
  • IP
  • IHC

    Supporting Data

    REACTIVITY H M R Mk Dm
    SENSITIVITY Endogenous
    MW (kDa) 38
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IHC-Immunohistochemistry 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 
    • Dm-D. melanogaster 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50
    Immunohistochemistry (Paraffin) 1:75 - 1:300

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-eIF2alpha (Ser51) RmAb detects endogenous eIF2alpha only when phosphorylated at Ser51. The antibody does not recognize elF2alpha phosphorylated at other sites. Human eIF2alpha residue Ser52 historically has been referenced as Ser51.

    Species Reactivity:

    Human, Mouse, Rat, Monkey, D. melanogaster

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser51 of human eIF2alpha.

    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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