|Application ||WB, IHC|
|Calculated MW||12580 Da|
|Other Names||Eukaryotic translation initiation factor 4E-binding protein 1, 4E-BP1, eIF4E-binding protein 1, Phosphorylated heat- and acid-stable protein regulated by insulin 1, PHAS-I, EIF4EBP1|
|Target/Specificity||A synthetic peptide corresponding to residues near the C-term of human4E-BP1 was used as immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||4E-BP1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways.|
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Provided below are standard protocols that you may find useful for product applications.
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 not (2). 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 64. Although, not all phosphorylation events equally block the 4EBP1-eIF4E interaction (3-4)
1. Pause, A., G.J. Belsham, A.-C. Gingras, O. Donz
2. Gingras, A.-C., S.G. Kennedy, M.A. O'Leary, N. Sonenberg, and N. Hay. 1998. Genes & Dev. 12: 502-513
3. Iritani, B. M., and Eisenman, R. N. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 13180
4. Trumpp, A., Refaeli, Y., Oskarsson, T., Gasser, S., Murphy, M., Martin, G. R., and Bishop, J. M. (2001) Nature 414, 768
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