Recombinant Human eIF4EBP1 protein (Tagged)
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Recombinant Human eIF4EBP1 protein (Tagged) is a Human Full Length protein, expressed in Escherichia coli, with >75%, suitable for SDS-PAGE, WB.
View Alternative 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
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human eIF4EBP1 protein (Tagged) (AB85248)
SDS-PAGE showing ab85248 at approximately 40kDa.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
EIF4EBP1 plays an important role in regulating cell growth and proliferation by modulating protein synthesis. It is a part of the eIF4F complex which is responsible for the initiation of mRNA translation. When hypophosphorylated eIF4EBP1 binds tightly to eIF4E and prevents the assembly of the active eIF4F complex leading to reduced translation initiation of mRNAs involved in growth and survival. This regulation is important in conditions where cells need to adapt to metabolic stress or external signals.
Pathways
The mammalian target of rapamycin (mTOR) pathway regulates eIF4EBP1 through phosphorylation. In response to growth signals mTOR phosphorylates eIF4EBP1 causing the release of eIF4E and allowing mRNA translation to proceed. This interaction links eIF4EBP1 to the PI3K/AKT/mTOR signaling pathway which influences cell cycle progression and survival. Related proteins in this pathway include ribosomal protein S6 kinase (S6K1) which is also phosphorylated by mTOR to promote protein synthesis.
Specifications
Form
Liquid
General info
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.
Sequence similarities
Belongs to the eIF4E-binding protein family.
Post-translational modifications
Phosphorylated on serine and threonine residues in response to insulin, EGF and PDGF (PubMed:12588975, PubMed:12747827, PubMed:22578813, PubMed:24403073, PubMed:29236692, PubMed:7935836, PubMed:9465032). Phosphorylation at Thr-37, Thr-46, Ser-65 and Thr-70, corresponding to the hyperphosphorylated form, is regulated by mTORC1 and abolishes binding to EIF4E (PubMed:12588975, PubMed:12747827, PubMed:22578813, PubMed:24403073, PubMed:29236692, PubMed:7935836, PubMed:9465032).. Ubiquitinated: when eIF4E levels are low, hypophosphorylated form is ubiquitinated by the BCR(KLHL25) complex, leading to its degradation and serving as a homeostatic mechanism to maintain translation and prevent eIF4E inhibition when eIF4E levels are low. Not ubiquitinated when hyperphosphorylated (at Thr-37, Thr-46, Ser-65 and Thr-70) or associated with eIF4E.
Target data
Product promise
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