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4E-BP1Phospho(pS65)(EIF4EBP1)antibody

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    4E-BP1 Phospho(pS65)(EIF4EBP1)antibody
    Cat.#: 2206-1
    Rabbit Monoclonal Antibody
    Clone ID: EP353(2)Y
    Swiss Prot: Q13541
    Mol Weight: 20kDa
    Size: 100ul

    Description
    4E-BP1 (eIF4E-binding protein) also known as PHAS, is a 10-12 kDa acidic protein that compete with eIF4G for binding of eiF4E to the mRNA 5 cap structure (1). Binding of the 4E-BPs to eIF4E is reversible and is dependent on the phosphorylation status of 4E-BP. Non-phosphorylated 4E-BP1 will bind strongly to eiF4E while, the phosphorylated form will no (2)t. Akt, TOR, MAP kinase, S6 kinase, and Cdc2 are known kinases capable of inactivating 4E-BP1 binding to eIF4E by phosphorylating either threonines 35, 45, 69 or serine 65. Although, not all phosphorylation events equally block the 4EBP1-eIF4E interaction (3-4)

    Recommended Applications
    WB

    Applications and Recommended Dilution Factors
    WB: 1:2000

    Species Reactivity
    Human, Mouse

    Cross reactivity determined by western blot only.

    Products Data


    A. Western blot analysis on NIH/3T3 cell lysates using anti-Phospho-4E-BP1 (pS65) (EIF4EBP1) RabMAb (cat. #2206-1). Cells were either (A) untreated (B) treated with PDGF.

    Specificity
    A phospho-specific peptide corresponding to residues surrounding serine 65 of human 4E-BP1 was used as an immunogen. This antibody detects 4E-BP1 phosphorylated at serine 65.

    Storage Condition and Buffer
    Store at -20 °C. Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. Stable for 12 months from date of receipt.

    Alternative Names
    EIF4EBP1 antibody, 4E-BP1 antibody, 4EBP1 antibody, BP-1 antibody, MGC4316 antibody, PHAS-I antibody, Eukaryotic translation initiation factor 4E-binding protein 1 antibody, Phosphorylated heat- and acid-stable protein regulated by insulin 1 antibody

    Description References
    1. Pause, A., 1994. Nature 371: 762-767
    2. Gingras, A.-C. 1998. Genes & Dev. 12: 502-513
    3. Iritani, B. M, (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 13180
    4. Trumpp, A., (2001) Nature 414, 768