| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EEF1D |
| Uniprot No | P29692 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-281aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMATNFLAHEKIWFDKFKYDDAERRFYEQMN GPVAGASRQENGASVILRDIARARENIQKSLAGSSGPGASSGTSGDHGEL VVRIASLEVENQSLRGVVQELQQAISKLEARLNVLEKSSPGHRATAPQTQ HVSPMRQVEPPAKKPATPAEDDEDDDIDLFGSDNEEEDKEAAQLREERLR QYAEKKAKKPALVAKSSILLDVKPWDDETDMAQLEACVRSIQLDGLVWGA SKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEHVQSVDIAAFNK I |
| 预测分子量 | 33 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EEF1D重组蛋白的3篇参考文献摘要(文献信息为模拟示例，供参考)：
1. **文献名称**: "Expression and purification of recombinant human EEF1D for structural studies"
**作者**: Zhang L, et al.
**摘要**: 本研究通过大肠杆菌系统成功表达并纯化了重组人源EEF1D蛋白，利用X射线晶体学分析其三维结构，揭示了其与GTP结合的关键结构域，为研究其在翻译延伸中的作用机制提供基础。
2. **文献名称**: "Functional characterization of EEF1D in cancer cell proliferation"
**作者**: Kim S, et al.
**摘要**: 通过重组EEF1D蛋白的体外功能实验，发现其过表达促进肿瘤细胞周期进展，并证实其通过与细胞周期蛋白CDK4的相互作用调控癌细胞增殖，提示其作为潜在治疗靶点。
3. **文献名称**: "EEF1D interacts with viral RNA polymerase: Insights from recombinant protein assays"
**作者**: Gomez-Reyes E, et al.
**摘要**: 利用重组EEF1D蛋白进行体外结合实验，发现其直接与流感病毒RNA聚合酶亚基PB1结合，可能通过干扰病毒复制复合体形成抑制感染过程。
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**备注**：以上内容为示例，实际文献需通过数据库(如PubMed、Web of Science)检索关键词“EEF1D recombinant protein”或“EEF1D expression”获取。建议结合具体研究方向筛选近年高相关性论文。
**Background of EEF1D Recombinant Protein**
EEF1D (Eukaryotic Translation Elongation Factor 1 Delta), also known as EF-1δ, is a critical subunit of the eukaryotic elongation factor-1 (EF-1) complex, which plays a central role in protein synthesis. The EF-1 complex facilitates the delivery of aminoacyl-tRNA to the ribosome during the elongation phase of translation. Specifically, EEF1D forms a stable subcomplex with EEF1Bγ, functioning as a guanine nucleotide exchange factor (GEF) that activates EF-1α by promoting the exchange of GDP for GTP, thereby sustaining translational efficiency.
Beyond its canonical role in translation, EEF1D is implicated in diverse cellular processes, including cytoskeletal regulation, cell cycle control, apoptosis, and signal transduction. Studies suggest its involvement in pathological conditions such as cancer, neurodegenerative disorders, and viral infections, where dysregulation of EEF1D expression or activity correlates with disease progression.
Recombinant EEF1D protein is engineered using expression systems (e.g., *E. coli* or mammalian cells) to produce high-purity, functional protein for research applications. Its recombinant form enables detailed study of molecular interactions, structural analysis, and mechanistic insights into translation elongation and non-canonical pathways. Researchers utilize EEF1D recombinant protein to explore its post-translational modifications (e.g., phosphorylation) and interactions with binding partners, which are crucial for understanding its multifunctional roles. Additionally, it serves as a tool for drug screening, antibody development, and diagnostic assays targeting diseases linked to translational dysregulation.
Overall, EEF1D recombinant protein is a vital resource for dissecting the molecular basis of protein synthesis and its broader implications in cellular homeostasis and disease.
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