| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EIF4E |
| Uniprot No | P06730 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-217aa |
| 氨基酸序列 | ATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV |
| 预测分子量 | 26.5 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. |
以下是关于EIF4E重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Structural Insights into the Eukaryotic Translation Initiation Factor eIF4E*
**作者**：Marcotrigiano, J. et al.
**摘要**：该研究通过X射线晶体学解析了人源EIF4E蛋白的三维结构，揭示了其与mRNA 5'帽结构结合的分子机制，为理解真核翻译起始机制提供了结构基础。
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2. **文献名称**：*eIF4E Promotes Nuclear Export of Cyclin D1 mRNAs via Interaction with CRM1*
**作者**：Topisirovic, I. et al.
**摘要**：研究发现重组EIF4E蛋白通过与核转运蛋白CRM1相互作用，调控细胞周期蛋白Cyclin D1 mRNA的核输出，揭示了EIF4E在肿瘤发生中促进增殖的机制。
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3. **文献名称**：*Targeting eIF4E in Cancer: A Phase I Trial of Ribavirin in Hematologic Malignancies*
**作者**：Assouline, S. et al.
**摘要**：临床试验表明，抗病毒药物利巴韦林通过抑制EIF4E活性，在白血病患者中显示出抗肿瘤效果，验证了EIF4E作为癌症治疗靶点的潜力。
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**补充说明**：
以上文献涵盖EIF4E的结构、功能及治疗应用，均为该领域的经典或关键研究。如需更近期文献(如2020年后)，建议检索PubMed或Web of Science获取最新进展。
**Background on eIF4E Recombinant Protein**
The eukaryotic initiation factor 4E (eIF4E) is a critical regulatory protein in mRNA translation, primarily responsible for recognizing the 5' cap structure (m7GpppN) of eukaryotic mRNAs. As a core component of the eIF4F complex, it collaborates with eIF4G and eIF4A to recruit ribosomes to mRNA, initiating protein synthesis. Dysregulation of eIF4E is linked to various diseases, including cancer, viral infections, and neurodevelopmental disorders, due to its role in controlling the translation of oncogenes, viral mRNAs, and other growth-related proteins.
Recombinant eIF4E is engineered using expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to produce purified, functional protein for research. This allows scientists to study its structure, binding interactions (e.g., with 4E-binding proteins [4E-BPs] or viral caps), and regulatory mechanisms. Recombinant variants often include tags (e.g., GST, His-tag) for easier purification and detection.
Key applications involve dissecting translation initiation pathways, screening inhibitors for therapeutic development (e.g., targeting eIF4E in cancers), and studying viral hijacking mechanisms (e.g., picornaviruses that cleave eIF4E). Structural studies using recombinant eIF4E have revealed insights into its cap-binding pocket and interaction interfaces, guiding drug design. Notably, eIF4E overexpression in tumors correlates with poor prognosis, making it a biomarker and therapeutic target.
Overall, recombinant eIF4E serves as a vital tool for unraveling translational control in health and disease, bridging molecular biology with translational medicine.
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