Render Target: STATIC
Render Timestamp: 2024-11-21T13:05:03.820Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-08-01 15:30:09.196
Product last modified at: 2024-11-15T13:00:23.508Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

4E-BP2 Antibody #2845

Filter:
  • WB
  • IP
  • IHC

    Supporting Data

    REACTIVITY H M R Mk B
    SENSITIVITY Endogenous
    MW (kDa) 15 to 20
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IHC-Immunohistochemistry 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 
    • B-Bovine 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100
    Immunohistochemistry (Paraffin) 1:200 - 1:800

    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

    4E-BP2 Antibody detects endogenous levels of total 4E-BP2, independent of phosphorylation. This antibody does not cross-react significantly with 4E-BP1.

    Species Reactivity:

    Human, Mouse, Rat, Monkey, Bovine

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues at the carboxy-terminus of human 4E-BP2. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Translation repressor protein 4E-BP1 (also known as PHAS-1) inhibits cap-dependent translation by binding to the translation initiation factor eIF4E. Hyperphosphorylation of 4E-BP1 disrupts this interaction and results in activation of cap-dependent translation (1). Both the PI3 kinase/Akt pathway and FRAP/mTOR kinase regulate 4E-BP1 activity (2,3). Multiple 4E-BP1 residues are phosphorylated in vivo (4). While phosphorylation by FRAP/mTOR at Thr37 and Thr46 does not prevent the binding of 4E-BP1 to eIF4E, it is thought to prime 4E-BP1 for subsequent phosphorylation at Ser65 and Thr70 (5).
    4E-BP2 and 4E-BP3 share high sequence homology with 4E-BP1, including conservation of the major FRAP/mTOR-dependent phosphorylation sites. Preliminary data suggests that phosphorylation of 4E-BP2 is regulated in a similar manner to that of 4E-BP1, although phosphorylation of this protein has not been as extensively studied (6).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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