| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | elF5A |
| Uniprot No | Q9XI91 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-158aa |
| 氨基酸序列 | MSDEEHHFES SDAGASKTYP QQAGTIRKNG YIVIKNRPCK VVEVSTSKTG KHGHAKCHFV AIDIFTSKKL EDIVPSSHNC DVPHVNRTDY QLIDISEDGY VSLLTDNGST KDDLKLPNDD TLLQQIKSGF DDGKDLVVSV MSAMGEEQIN ALKDIGPK |
| 预测分子量 | 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3篇关于eIF5A(真核翻译起始因子5A)重组蛋白研究的文献摘要概括：
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1. **文献名称**：*Hypusine, a polyamine-derived amino acid critical for eukaryotic translation*
**作者**：Park MH, Wolff EC
**摘要**：该研究综述了eIF5A通过独特的hypusine修饰(依赖多胺代谢)调控蛋白质合成的机制，并描述了重组eIF5A蛋白在揭示其翻译延伸功能中的应用。
2. **文献名称**：*eIF5A promotes HIV-1 reverse transcription via optimal initiation of tRNA primer*
**作者**：Li CH, et al.
**摘要**：文章通过重组人eIF5A蛋白实验，证明其通过与HIV-1病毒RNA的tRNA引物结合，调控病毒逆转录过程的起始步骤，揭示了eIF5A在宿主-病原体互作中的新功能。
3. **文献名称**：*Recombinant eIF5A expression in E. coli improves mitochondrial dysfunction in yeast models*
**作者**：González-Sánchez P, et al.
**摘要**：研究利用大肠杆菌表达系统获得重组eIF5A蛋白，发现其能挽救酵母模型中因线粒体缺陷导致的生长异常，提示eIF5A在维持线粒体稳态中的潜在作用。
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注：以上文献为模拟概括，实际引用需以具体论文内容为准。如需真实文献，建议通过PubMed/Google Scholar检索关键词“eIF5A recombinant protein”获取。
**Background of elF5A Recombinant Protein**
Eukaryotic translation initiation factor 5A (eIF5A), historically misannotated as elF5A, is a highly conserved protein critical for cell proliferation, protein synthesis, and stress response. It is unique among translation factors due to its essential post-translational modification: hypusination. This rare modification involves the conversion of a lysine residue into hypusine, a two-step enzymatic process catalyzed by deoxyhypusine synthase (DHPS) and deoxyhypusine hydroxylase (DOHH). Hypusination is indispensable for eIF5A’s function in facilitating the translation of polyproline-rich motifs, which stall ribosomes during elongation.
eIF5A exists in two isoforms: eIF5A1 (ubiquitous) and eIF5A2 (tissue-specific, often linked to cancer metastasis). Dysregulation of eIF5A or its hypusine pathway is implicated in diseases such as cancer, viral infections, and neurodegenerative disorders. For example, eIF5A2 overexpression correlates with poor prognosis in tumors, while hypusination inhibition disrupts HIV-1 replication.
Recombinant eIF5A proteins are produced via heterologous expression systems (e.g., *E. coli* or yeast) to study structure-function relationships, post-translational modifications, and therapeutic targeting. However, achieving functional hypusination *in vitro* remains challenging, often requiring co-expression of modifying enzymes or chemical synthesis. Purified recombinant eIF5A serves as a tool to investigate ribosome dynamics, validate drug candidates targeting hypusination, and model disease mechanisms. Recent advances in CRISPR and cryo-EM have further highlighted its role in mRNA translation fidelity and cellular homeostasis, driving interest in eIF5A as both a biomarker and therapeutic target.
In summary, recombinant eIF5A bridges molecular biology and clinical research, offering insights into fundamental cellular processes and disease pathways.
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