| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | tetX3 |
| Uniprot No | Q7X2A0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-378aa |
| 氨基酸序列 | MTLLKYKKITIIGAGPVGLTMARLLQQNGVDITVYERDKDQDARIFGGTLDLHRDSGQEAMKRAGLLQTYYDLALPMGVNIVDEKGNILTTKNVRPENRFDNPEINRNDLRTILLNSLQNDTVIWDRKLVTLEPDKEKWILTFGDKSSETADLVIIANGGMSKVRKFVTDTEVEETGTFNIQADIHQPEVNCPGFFQLCNGNRLMAAHQGNLLFANPNNNGALHFGISFKTPDEWKSKTQVDFQDRNSVVDFLLKKFSDWDERYKELIRLTSSFVGLATRIFPLDKSWKSKRPLPITMIGDAAHLMPPFAGQGVNSGLMDALILSDNLTNGKFNSIEEAIENYEQQMFAYGREAQTESIINETEMFSLDFSFQKLMNL |
| 预测分子量 | 46.3 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. |
以下为模拟生成的3篇关于tetX3重组蛋白的假想参考文献示例(实际文献需通过学术数据库检索)：
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1. **"Functional Characterization of Recombinant TetX3: A Novel Tetracycline-Inactivating Enzyme"**
*Zhang, L. et al. (2020)*
摘要：本研究在大肠杆菌中重组表达了TetX3蛋白，证实其通过羟基化作用降解四环素类抗生素，酶动力学分析显示其对多西环素的催化效率高于其他同源酶，为耐药机制研究提供依据。
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2. **"Crystal Structure of TetX3 Reveals Substrate-Binding Specificity"**
*Wang, Y. et al. (2018)*
摘要：首次解析了TetX3重组蛋白的晶体结构(2.1 Å)，发现其活性中心独特的疏水口袋设计，解释了其对第三代四环素类药物的高亲和力，结构信息为抑制剂开发奠定基础。
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3. **"Heterologous Expression and Antibiotic Resistance Profile of TetX3 in Gram-Negative Pathogens"**
*Chen, H. & Li, X. (2021)*
摘要：通过质粒载体将tetX3基因导入肺炎克雷伯菌，证明重组TetX3蛋白可赋予宿主对米诺环素等药物的高水平耐药性，揭示了该基因在临床菌株中的潜在传播风险。
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提示：以上为模拟内容，实际文献建议通过PubMed/Google Scholar检索关键词 "tetX3 recombinant protein" "tetracycline resistance enzyme" 获取。已知真实相关研究多聚焦于四环素修饰酶(如TetX)的进化与功能扩展。
TetX3 is a recombinant protein derived from the tetracycline-inactivating enzyme TetX, originally identified in anaerobic bacteria such as *Bacteroides* species. TetX enzymes belong to a family of flavin-dependent monooxygenases that chemically modify tetracycline antibiotics, rendering them ineffective by hydroxylation. This mechanism contributes to tetracycline resistance, a growing concern in antimicrobial resistance (AMR) research. TetX3. a variant of TetX, exhibits enhanced activity against later-generation tetracyclines, including tigecycline, a broad-spectrum antibiotic considered a last-resort treatment for multidrug-resistant infections.
The recombinant TetX3 protein is typically produced via heterologous expression in *E. coli* or other microbial systems, enabling large-scale purification for biochemical and structural studies. Its engineered form often includes affinity tags (e.g., His-tags) to facilitate purification. Researchers study TetX3 to understand its substrate specificity, catalytic mechanism, and role in conferring resistance. Structural analyses using X-ray crystallography or cryo-EM have revealed key domains, including a flavin adenine dinucleotide (FAD)-binding site and a substrate-binding pocket, which undergo conformational changes during catalysis.
Interest in TetX3 extends to clinical and environmental monitoring, as its gene can be horizontally transferred among pathogens via mobile genetic elements. Studies also explore its potential as a biotechnological tool, such as in degrading tetracycline residues in contaminated environments. Additionally, TetX3 serves as a model for developing tetracycline analogs resistant to enzymatic inactivation or designing inhibitors to counteract resistance. Its characterization underscores the evolutionary adaptability of microbial enzymes and informs strategies to combat AMR, highlighting the interplay between antibiotic use, bacterial genetics, and public health challenges.
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