|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||The synthetic peptide sequence used to generate the antibody AP3473a was selected from the region of human Phospho-EIF4EBP1-S111. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. 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.
EIF4EBP1 is a member of a family of translation repressor proteins. This protein directly interacts with eukaryotic translation initiation factor 4E (eIF4E), which is a limiting component of the multisubunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs. Interaction of EIF4EBP1 with eIF4E inhibits complex assembly and represses translation. EIF4EBP1 is phosphorylated in response to various signals including UV irradiation and insulin signaling, resulting in its dissociation from eIF4E and activation of mRNA translation.
Fonseca,B.D., J. Biol. Chem. 282 (34), 24514-24524 (2007)Armengol,G., Cancer Res. 67 (16), 7551-7555 (2007)
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