Render Target: STATIC
Render Timestamp: 2024-11-21T13:21:31.504Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-08-01 15:24:34.831
Product last modified at: 2024-11-06T20:15:13.688Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-eIF4B (Ser406) Antibody #5399

Filter:
  • WB
  • IP
  • IF

    Supporting Data

    REACTIVITY H M
    SENSITIVITY Endogenous
    MW (kDa) 80
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50
    Immunofluorescence (Immunocytochemistry) 1:50

    Storage

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

    Protocol

    Specificity / Sensitivity

    Phospho-eIF4B (Ser406) Antibody detects endogenous levels of eIF4B protein only when phosphorylated at Ser406.

    Species Reactivity:

    Human, Mouse

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Rat

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser406 of human eIF4B protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Eukaryotic initiation factor 4B (eIF4B) is thought to assist the eIF4F complex in translation initiation. In plants, eIF4B is known to interact with the poly-(A) binding protein, increasing its poly-(A) binding activity (1). Heat shock and serum starvation cause dephosphorylation of eIF4B at multiple sites with kinetics similar to those of the corresponding inhibition of translation, while phosphorylation of eIF4B following insulin treatment correlates well with an observed increase in translation (2-5). Multiple kinases, including p70 S6 kinase, can phosphorylate eIF4B in vitro, and at least one serum-inducible eIF4B phosphorylation site is sensitive to rapamycin and LY294002 (6). Recently, Ser406 was identified as a novel phosphorylation site regulated by mitogens (7), and the phosphorylation of this site is dependent on MEK and mTOR activity (7). This phosphorylation is shown to be essential for the translational activity of eIF4B (7).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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