EIF4EBP2 Blocking Peptide (C-term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q13542 |
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Other Accession | NP_004087.1 |
Gene ID | 1979 |
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Other Names | Eukaryotic translation initiation factor 4E-binding protein 2, 4E-BP2, eIF4E-binding protein 2, EIF4EBP2 |
Target/Specificity | The synthetic peptide sequence is selected from aa 102-115 of HUMAN EIF4EBP2 |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
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. |
Name | EIF4EBP2 (HGNC:3289) |
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Function | Repressor of translation initiation involved in synaptic plasticity, learning and memory formation (PubMed:30765518). Regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form of EIF4EBP2 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 (PubMed:30765518, PubMed:25533957). EIF4EBP2 is enriched in brain and acts as a regulator of synapse activity and neuronal stem cell renewal via its ability to repress translation initiation (By similarity). Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (By similarity). |
Cellular Location | Cytoplasm {ECO:0000250|UniProtKB:P70445}. Nucleus {ECO:0000250|UniProtKB:P70445} |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a member of the eukaryotic translation initiation factor 4E binding protein family. The gene products of this family bind eIF4E and inhibit translation initiation. However, insulin and other growth factors can release this inhibition via a phosphorylation-dependent disruption of their binding to eIF4E. Regulation of protein production through these gene products have been implicated in cell proliferation, cell differentiation and viral infection.
References
Bailey, S.D., et al. Diabetes Care (2010) In press :
Bidinosti, M., et al. J. Biol. Chem. 285(25):19402-19408(2010)
Johnatty, S.E., et al. PLoS Genet. 6 (7), E1001016 (2010) :
Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)
Gingras, A.C., et al. Virology 237(1):182-186(1997)
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