Render Target: STATIC
Render Timestamp: 2024-12-23T12:11:34.417Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:53:39.173
Product last modified at: 2024-11-02T14:00:08.817Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

eIF4B (1F5) Mouse mAb #13088

Filter:
  • WB
  • IHC
  • IF

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 80
    Source/Isotype Mouse IgG2b
    Application Key:
    • WB-Western Blotting 
    • IHC-Immunohistochemistry 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunohistochemistry (Paraffin) 1:100
    Immunofluorescence (Immunocytochemistry) 1:100

    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

    eIF4B (1F5) Mouse mAb recognizes endogenous levels of total eIF4B protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a recombinant fragment around Val473 of human eIF4B protein.

    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).
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