| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | tusA |
| Uniprot No | Q9I3F3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-79aa |
| 氨基酸序列 | MTHSVDAILDATGLNCPEPVMMLHNKVRDLAPGGLLKVIATDPSTRRDIPKFCVFLGHELVEQQEEAGTYLYWIRKKAD |
| 预测分子量 | 16.3 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 **TusA重组蛋白** 的模拟参考文献示例(基于典型研究内容整理，建议通过学术数据库获取具体文献)：
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1. **文献名称**：*"Recombinant TusA Protein in Bacterial Sulfur Metabolism: Cloning and Functional Analysis"*
**作者**：Smith J, et al.
**摘要**：研究通过大肠杆菌表达重组TusA蛋白，验证其参与硫转移反应，并证明其与IscS酶的相互作用对tRNA硫修饰的关键作用。
2. **文献名称**：*"Structural Characterization of TusA in Selenocysteine Biosynthesis"*
**作者**：Li Y, et al.
**摘要**：利用X射线晶体学解析重组TusA蛋白的三维结构，揭示其结合硒代半胱氨酸前体的活性位点，阐明其在硒代谢中的分子机制。
3. **文献名称**：*"TusA Recombinant Expression and Its Role in Oxidative Stress Response"*
**作者**：Zhang R, et al.
**摘要**：通过重组TusA蛋白的体外实验，证明其通过调节硫醇化反应增强细菌对氧化应激的耐受性，为抗逆机制研究提供依据。
4. **文献名称**：*"Functional Redundancy of TusA-like Proteins in Archaea"*
**作者**：Müller S, et al.
**摘要**：比较不同古菌中TusA重组蛋白的功能，发现其与细菌TusA的硫转移活性相似，但存在物种特异性底物偏好。
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**注意**：以上为模拟示例，实际文献需通过PubMed、Web of Science或Google Scholar等平台，以关键词“TusA recombinant protein”、“TusA sulfur metabolism”等检索获取。
**Background of TusA Recombinant Protein**
TusA (thiouridine synthase A) is a small, conserved protein involved in sulfur transfer pathways, primarily known for its role in post-transcriptional modification of transfer RNA (tRNA). In *Escherichia coli* and other bacteria, TusA participates in the synthesis of 4-thiouridine (s⁴U), a modified nucleoside critical for tRNA stability, stress response, and cellular redox sensing. It acts as a sulfur carrier, collaborating with enzymes like IscS to incorporate sulfur into tRNA molecules. Beyond tRNA thiolation, TusA is implicated in broader sulfur metabolism, including iron-sulfur (Fe-S) cluster biosynthesis and molybdenum cofactor assembly, linking it to essential metabolic and regulatory processes.
Recombinant TusA protein is engineered for overexpression and purification in heterologous systems (e.g., *E. coli*), enabling structural and functional studies. Its compact size (~14 kDa) and solubility facilitate biochemical characterization, such as elucidating sulfur transfer mechanisms or protein-protein interactions within multi-enzyme complexes. TusA’s role in microbial stress adaptation and virulence has also spurred interest in pathogenic species, where it may serve as a potential antimicrobial target.
Structural analyses (e.g., X-ray crystallography, NMR) reveal TusA’s conserved thioredoxin-like fold and key residues involved in sulfur trafficking. Recent studies explore its interplay with other sulfur-relay proteins (e.g., TusBCD, MnmA) and regulatory roles in bacterial persistence under oxidative stress. Recombinant TusA is further utilized in enzymology, drug discovery, and synthetic biology, offering insights into sulfur-based post-transcriptional regulation and novel therapeutic strategies against bacterial infections.
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