| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EIF4EBP1 |
| Uniprot No | Q13541 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-118aa |
| 氨基酸序列 | SGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI |
| 预测分子量 | 19.4kDa |
| 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EIF4EBP1重组蛋白的3篇代表性文献摘要：
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1. **文献名称**：*Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism*
**作者**：Gingras, A.C., et al.
**摘要**：该研究通过重组表达的4E-BP1蛋白，揭示了mTORC1调控其磷酸化的两阶段机制，发现不同位点的磷酸化顺序影响其与eIF4E的结合能力，进而调控翻译起始。
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2. **文献名称**：*Structure of the eukaryotic initiation factor eIF4E in complex with 4E-BP1*
**作者**：Marcotrigiano, J., et al.
**摘要**：通过重组表达并纯化人源4E-BP1和eIF4E蛋白，解析了二者复合物的晶体结构，阐明了4E-BP1通过保守基序竞争性抑制eIF4E与其他翻译因子的结合。
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3. **文献名称**：*mTOR inhibition induces upstream receptor tyrosine kinase signaling and activates Akt*
**作者**：Hara, K., et al.
**摘要**：利用重组4E-BP1蛋白进行体外激酶实验，证明mTOR抑制剂可解除4E-BP1的磷酸化，并激活负反馈环路，导致Akt信号通路的意外增强。
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**备注**：以上文献均涉及重组EIF4EBP1的表达与应用，涵盖磷酸化调控、结构解析及信号通路机制研究，适合作为该蛋白功能研究的理论基础。如需扩展，可进一步检索近年关于4E-BP1重组蛋白在疾病模型(如癌症、代谢疾病)中的应用研究。
**Background of EIF4EBP1 Recombinant Protein**
EIF4EBP1 (Eukaryotic Translation Initiation Factor 4E-Binding Protein 1), also known as 4E-BP1. is a key regulatory protein involved in controlling mRNA translation initiation, a critical step in protein synthesis. It functions as a suppressor of cap-dependent translation by binding to eukaryotic initiation factor 4E (eIF4E), a component of the eIF4F complex essential for recruiting ribosomes to mRNA. This interaction is modulated by phosphorylation: under nutrient-rich conditions, the mTORC1 (mechanistic target of rapamycin complex 1) pathway phosphorylates EIF4EBP1. releasing it from eIF4E and enabling translation. During stress or nutrient deprivation, hypophosphorylated EIF4EBP1 binds tightly to eIF4E, inhibiting the assembly of the translation machinery.
Recombinant EIF4EBP1 protein is produced through genetic engineering, typically expressed in *E. coli* or mammalian cell systems, and purified for research applications. It retains the functional domains required for interacting with eIF4E and undergoing phosphorylation/dephosphorylation. Researchers utilize this protein to study mTOR signaling dynamics, cellular stress responses, and mechanisms underlying diseases like cancer, where dysregulated translation is common. Mutant variants (e.g., non-phosphorylatable or hyperphosphorylated mimics) are also engineered to dissect structure-function relationships.
As a tool, recombinant EIF4EBP1 aids in drug discovery, particularly for therapies targeting mTOR or translation initiation pathways. Its role in aging, metabolic disorders, and tumor progression underscores its biomedical relevance, making it a focal point in studies aiming to modulate protein synthesis for therapeutic benefit.
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