| 纯度 | >90%SDS-PAGE. |
| 种属 | Clostridium tetani |
| 靶点 | tetX |
| Uniprot No | P04958 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-864aa |
| 氨基酸序列 | MPITINNFRYSDPVNNDTIIMMEPPYCKGLDIYYKAFKITDRIWIVPERYEFGTKPEDFNPPSSLIEGASEYYDPNYLRTDSDKDRFLQTMVKLFNRIKNNVAGEALLDKIINAIPYLGNSYSLLDKFDTNSNSVSFNLLEQDPSGATTKSAMLTNLIIFGPGPVLNKNEVRGIVLRVDNKNYFPCRDGFGSIMQMAFCPEYVPTFDNVIENITSLTIGKSKYFQDPALLLMHELIHVLHGLYGMQVSSHEIIPSKQEIYMQHTYPISAEELFTFGGQDANLISIDIKNDLYEKTLNDYKAIANKLSQVTSCNDPNIDIDSYKQIYQQKYQFDKDSNGQYIVNEDKFQILYNSIMYGFTEIELGKKFNIKTRLSYFSMNHDPVKIPNLLDDTIYNDTEGFNIESKDLKSEYKGQNMRVNTNAFRNVDGSGLVSKLIGLCKKIIPPTNIRENLYNRTASLTDLGGELCIKIKNEDLTFIAEKNSFSEEPFQDEIVSYNTKNKPLNFNYSLDKIIVDYNLQSKITLPNDRTTPVTKGIPYAPEYKSNAASTIEIHNIDDNTIYQYLYAQKSPTTLQRITMTNSVDDALINSTKIYSYFPSVISKVNQGAQGILFLQWVRDIIDDFTNESSQKTTIDKISDVSTIVPYIGPALNIVKQGYEGNFIGALETTGVVLLLEYIPEITLPVIAALSIAESSTQKEKIIKTIDNFLEKRYEKWIEVYKLVKAKWLGTVNTQFQKRSYQMYRSLEYQVDAIKKIIDYEYKIYSGPDKEQIADEINNLKNKLEEKANKAMININIFMRESSRSFLVNQMINEAKKQLLEFDTQSKNILMQYIKANSKFIGITELKKLESKINKVFSTPIPFSYS |
| 预测分子量 | 105.1 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篇与tetX重组蛋白相关的参考文献概览：
1. **《Functional Characterization of the TetX Enzyme Involved in Tetracycline Resistance》**
- 作者：Smith J, et al.
- 摘要：研究通过大肠杆菌重组表达了tetX编码的酶，揭示了其对四环素类抗生素(如强力霉素)的羟基化修饰机制，阐明了其通过氧化作用降解药物的分子基础。
2. **《Structural Insights into TetX-Mediated Antibiotic Inactivation》**
- 作者：Li Y, et al.
- 摘要：利用X射线晶体学解析了重组TetX蛋白的三维结构，发现其活性位点含有黄素辅因子，解释了其依赖NADPH的催化活性，为设计新型四环素类抗生素提供了结构依据。
3. **《Heterologous Expression and Biochemical Analysis of TetX2 from Bacteroides》**
- 作者：Wang H, et al.
- 摘要：在枯草芽孢杆菌中重组表达TetX2蛋白，证实其对四环素、米诺环素的高效修饰能力，并发现该酶在厌氧环境下的稳定性，提示其在肠道菌群耐药性传播中的作用。
注：以上文献名为示例，实际研究可参考《Antimicrobial Agents and Chemotherapy》《Journal of Molecular Biology》等期刊中关于四环素耐药酶机制的论文。
TetX is a recombinantly produced enzyme that plays a significant role in bacterial antibiotic resistance, particularly against tetracycline-class antibiotics. Originally identified in pathogenic bacteria, the tetX gene encodes a flavin-dependent monooxygenase that chemically modifies tetracycline molecules through hydroxylation, rendering them ineffective against bacterial targets. This mechanism differs from other tetracycline resistance genes (e.g., tetA or tetM) that primarily mediate efflux pumps or ribosomal protection.
The recombinant TetX protein is engineered through cloning and expressing the tetX gene in heterologous systems like E. coli. This allows large-scale production for structural and functional studies. Researchers purify the protein using affinity tags (e.g., His-tag) to investigate its catalytic activity, substrate specificity, and interaction with tetracycline derivatives. Its recombinant form has become a valuable tool for understanding resistance evolution and developing tetracycline analogs resistant to enzymatic inactivation.
Studies on recombinant TetX have revealed its broad substrate spectrum, including newer-generation tetracyclines like tigecycline, highlighting its clinical relevance in emerging resistance. Structural analyses using X-ray crystallography and mutagenesis have identified key residues in its active site, guiding the design of enzyme inhibitors. Additionally, recombinant TetX serves as a biomarker in environmental and clinical surveillance to detect tetX-carrying pathogens.
Ongoing research focuses on balancing the enzyme's biochemical characterization with translational applications, aiming to counteract resistance while preserving tetracycline's therapeutic value. Its study exemplifies the interplay between microbial adaptation and biotechnological innovation in addressing antibiotic resistance challenges.
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