|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 phospho specific peptide corresponding to residues surrounding threonine 70 was used as an immunogen. This antibody detects 4E-BP1 phosophorylated at threonine 70.|
|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 Phospho (pT70) 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 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, 70 or serine 64. Although, not all phosphorylation events equally block the 4EBP1-eIF4E interaction (3-4)
1. Pause, A., et al. 1994. Nature 371: 762-767
2. Gingras, A.-C., et al. Genes & Dev. 12: 502-513, 1998
3. Iritani, BM et al. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 13180
4. Trumpp, A. et al. Nature 414, 768
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