Recombinant Human 4E-BP2 protein is a Human Full Length protein, in the 1 to 120 aa range, expressed in Escherichia coli, with >95% purity, = 1 EU/µg endotoxin level and suitable for SDS-PAGE.
M S S S A G S G H Q P S Q S R A I P T R T V A I S D A A Q L P H D Y C T T P G G T L F S T T P G G T R I I Y D R K F L L D R R N S P M A Q T P P C H L P N I P G V T S P G T L I E D S K V E V N N L N N L N N H D R K H A V G D D A Q F E M D I
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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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:25533957, PubMed:30765518). 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).
Eukaryotic translation initiation factor 4E-binding protein 2, 4E-BP2, eIF4E-binding protein 2, EIF4EBP2
Recombinant Human 4E-BP2 protein is a Human Full Length protein, in the 1 to 120 aa range, expressed in Escherichia coli, with >95% purity, = 1 EU/µg endotoxin level and suitable for SDS-PAGE.
pH: 8
Constituents: 99% Tris-HCl buffer, 0.88% Sodium chloride
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:25533957, PubMed:30765518). 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).
Belongs to the eIF4E-binding protein family.
Phosphorylation at Thr-37, Thr-46, Ser-65, Thr-70 and Ser-83 is mediated by MTOR and corresponds to the hyperphosphorylated form: it abolishes binding to EIF4E by inducing folding of intrinsically disordered regions (PubMed:24207126, PubMed:25533957). First phosphorylated at Thr-37 and Thr-46 by MTOR, inducing folding of region encompassing residues from Pro-18 to Arg-62 of into a four-stranded beta-domain that sequesters the helical YXXXXLPhi motif into a partly buried beta-strand, blocking accessibility to EIF4E. Protein phosphorylated at Thr-37 and Thr-46 is however unstable and subsequent phosphorylation at Ser-65, Thr-70 and Ser-83 is required to stabilize the fold, decreasing affinity for EIF4E by a factor of 4000 (PubMed:24207126, PubMed:25533957). Phosphorylated in response to insulin, EGF and PDGF.
0.2 μM filtered solution.
The 4E-BP2 protein also known as eukaryotic translation initiation factor 4E-binding protein 2 is an important regulator of translation initiation. It is a small protein with a molecular weight of approximately 14 kDa. 4E-BP2 is expressed in various tissues with a prominent presence in the brain. This protein binds to eukaryotic initiation factor 4E (eIF4E) inhibiting the initiation of cap-dependent translation by preventing eIF4E from assembling into the larger eIF4F complex.
The 4E-BP2 protein inhibits the initiation of protein synthesis regulating gene expression at a translational level. 4E-BP2 does not form part of a stable complex but transiently interacts with eIF4E in response to different cellular signals. When 4E-BP2 is phosphorylated by mammalian target of rapamycin (mTOR) it undergoes a conformational change that weakens its binding to eIF4E allowing protein synthesis to proceed. This regulation exhibits tissue specificity and involves responses to growth factors nutrients and cellular stress.
The involvement of 4E-BP2 is important in the mTOR signaling pathway a central pathway regulating cell growth and metabolism in response to environmental cues. The mTOR pathway includes other proteins like eIF4E which 4E-BP2 interacts with directly and mTOR itself which phosphorylates 4E-BP2. Additionally 4E-BP2 also participates in the insulin signaling pathway influencing how cells respond to insulin and other growth factors by regulating protein translation.
Altered 4E-BP2 function has implications in neurological disorders and cancer. In the brain dysregulation of 4E-BP2 is associated with autism spectrum disorders as its role in neural development and plasticity is important. In cancer aberrant activity of 4E-BP2 can lead to unchecked cellular proliferation due to disrupted control of protein synthesis. The protein's regulation by mTOR links it to various cancers as increased mTOR activity can result in decreased 4E-BP2 activity facilitating tumorigenesis.
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SDS-PAGE analysis of ab172157 in 1) Non reducing and 2) Reducing conditions.
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