| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ytfE |
| Uniprot No | P69506 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-220aa |
| 氨基酸序列 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMDHISLENNVLFPRALAGE |
| 预测分子量 | 51.9 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ytfE重组蛋白的3篇参考文献及其摘要概述：
1. **文献名称**：*"Characterization of the ytfE Gene Product in Escherichia coli: A Role in Iron Metabolism"*
**作者**：Smith A, et al.
**摘要**：研究证实ytfE编码的铁硫蛋白参与大肠杆菌的铁稳态调控，重组蛋白体外实验显示其具有铁离子结合能力，可能参与氧化应激下的铁再分配。
2. **文献名称**：*"Structural and Functional Analysis of Recombinant YtfE Protein from Escherichia coli"*
**作者**：Zhang L, et al.
**摘要**：通过X射线晶体学解析ytfE重组蛋白的三维结构，揭示其独特的二聚体构象及可能的活性位点，功能实验表明其具有超氧化物歧化酶样活性。
3. **文献名称**：*"Expression and Purification of Recombinant YtfE in E. coli for Biotechnological Applications"*
**作者**：Kim H, Patel R.
**摘要**：优化ytfE重组蛋白在大肠杆菌中的可溶性表达条件，建立高效纯化流程，并验证其在体外作为抗氧化酶的应用潜力。
4. **文献名称**：*"YtfE: A Novel Player in Bacterial Oxidative Stress Defense through Iron-Sulfur Cluster Repair"*
**作者**：Molina-Quiroz RC, et al.
**摘要**：证明ytfE通过修复氧化损伤的铁硫簇维持呼吸链酶活性，重组蛋白回补实验显著提高ΔytfE菌株对H₂O₂的抗性。
注：以上文献信息为示例性内容，实际研究中建议通过PubMed或Web of Science以"ytfE recombinant protein"为关键词检索最新论文。
The ytfE protein, originally identified in *Escherichia coli*, is a conserved bacterial protein implicated in iron metabolism and stress response pathways. It belongs to the YtfE family, which shares structural homology with di-iron carboxylate proteins involved in redox reactions. YtfE is proposed to function as a repair enzyme for iron-sulfur (Fe-S) clusters, critical cofactors in numerous cellular processes, including electron transport and DNA repair. Under oxidative stress or iron-limiting conditions, Fe-S clusters are prone to damage, and YtfE may facilitate their reconstitution, thereby maintaining metabolic homeostasis. Genomic studies suggest its role in bacterial survival during host infection, linking it to pathogenicity in some strains.
Recombinant YtfE protein is engineered through heterologous expression systems, typically using *E. coli* as a host. The gene encoding YtfE is cloned into expression vectors under inducible promoters, enabling high-yield production. Purification often involves affinity chromatography tags (e.g., His-tags) followed by functional validation. Structural analyses reveal YtfE forms a homodimer with a non-heme di-iron center, essential for its enzymatic activity. Biochemical studies demonstrate its ability to bind nitric oxide (NO), suggesting a dual role in Fe-S repair and NO detoxification, which may mitigate nitrosative stress during infections.
Research on recombinant YtfE has broad applications. It serves as a model to study Fe-S cluster biogenesis and repair mechanisms, with implications for understanding bacterial stress adaptation. Its NO-binding properties are explored for potential antimicrobial strategies, as disrupting YtfE could sensitize pathogens to host immune defenses. Additionally, recombinant YtfE aids in structural biology, providing insights into di-iron protein engineering for biotechnological applications, such as biosensors or biocatalysts. Despite progress, its exact physiological substrates and regulatory mechanisms remain under investigation, highlighting its relevance in microbial physiology and infection biology.
×
