| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EIF4EBP2 |
| Uniprot No | Q13542 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-120aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSSSAGSGHQPSQSRAIPTRTVAISDAAQL PHDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPG VTSPGTLIEDSKVEVNNLNNLNNHDRKHAVGDDAQFEMDI |
| 预测分子量 | 15 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
1. **"Structural insights into the regulation of EIF4EBP2 by phosphorylation"**
*作者：Smith J, et al. (Journal of Biological Chemistry, 2020)*
**摘要**：通过X射线晶体学解析了重组人源EIF4EBP2蛋白的磷酸化依赖性构象变化，揭示了其与eIF4E结合的分子机制及mTOR信号通路的调控作用。
2. **"EIF4EBP2重组蛋白在癌症细胞翻译抑制中的功能研究"**
*作者：Li X, et al. (Oncogene, 2018)*
**摘要**：利用重组EIF4EBP2蛋白证实其过表达可竞争性抑制eIF4E与mRNA 5'帽结构结合，进而阻断癌细胞的蛋白质翻译并诱导凋亡。
3. **"Dynamic interaction of EIF4EBP2 with mTORC1 in nutrient sensing"**
*作者：Zhang Y, et al. (Cell Reports, 2019)*
**摘要**：通过体外重组蛋白实验，证明EIF4EBP2的磷酸化状态受mTORC1调控，并参与细胞对氨基酸缺乏的应激响应，影响自噬与增殖平衡。
4. **"EIF4EBP2重组蛋白在神经退行性疾病模型中的保护作用"**
*作者：Wang R, et al. (Molecular Neurobiology, 2021)*
**摘要**：在阿尔茨海默病细胞模型中，重组EIF4EBP2蛋白通过抑制异常蛋白翻译，减少tau蛋白过度磷酸化，缓解神经元损伤。
(注：上述文献为示例性质，实际引用需以真实发表文章为准。)
The eukaryotic translation initiation factor 4E-binding protein 2 (EIF4EBP2) is a member of the EIF4E-binding protein family that regulates cap-dependent protein synthesis by interacting with eukaryotic initiation factor 4E (eIF4E). As a key downstream effector of the mTOR signaling pathway, EIF4EBP2 undergoes phosphorylation in response to growth signals, modulating its ability to sequester eIF4E and thereby controlling the initiation of mRNA translation. Dysregulation of EIF4EBP2 has been implicated in various pathological conditions, including cancer, where aberrant protein synthesis drives uncontrolled cell proliferation.
Recombinant EIF4EBP2 proteins are engineered to study its structural and functional properties, typically expressed in bacterial or mammalian systems with affinity tags for purification. These proteins retain critical phosphorylation sites (e.g., Thr37/Thr46) and domains required for eIF4E binding, enabling investigations into mTOR-mediated signaling cascades and translational control mechanisms. Researchers utilize recombinant EIF4EBP2 to dissect its role in cellular stress responses, metabolic regulation, and oncogenesis through in vitro binding assays, kinase activity studies, or cellular overexpression models.
The development of recombinant EIF4EBP2 also supports drug discovery efforts, particularly for therapies targeting mTOR pathway hyperactivity in cancers and metabolic disorders. By mimicking or inhibiting its phosphorylation status, these proteins help identify small molecules that restore normal translation regulation. Additionally, isoform-specific studies using recombinant EIF4EBP2 (versus EIF4EBP1/3) clarify distinct biological roles, given their differential tissue expression and binding affinities. Overall, recombinant EIF4EBP2 serves as a vital tool for unraveling translational control networks and developing precision therapeutics.
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