| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RDX |
| Uniprot No | P35241 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-583aa |
| 氨基酸序列 | MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTVGLR EVWFFGLQYV DSKGYSTWLK LNKKVTQQDV KKENPLQFKF RAKFFPEDVS EELIQEITQR LFFLQVKEAI LNDEIYCPPE TAVLLASYAV QAKYGDYNKE IHKPGYLAND RLLPQRVLEQ HKLTKEQWEE RIQNWHEEHR GMLREDSMME YLKIAQDLEM YGVNYFEIKN KKGTELWLGV DALGLNIYEH DDKLTPKIGF PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI EVQQMKAQAR EEKHQKQLER AQLENEKKKR EIAEKEKERI EREKEELMER LKQIEEQTIK AQKELEEQTR KALELDQERK RAKEEAERLE KERRAAEEAK SAIAKQAADQ MKNQEQLAAE LAEFTAKIAL LEEAKKKKEE EATEWQHKAF AAQEDLEKTK EELKTVMSAP PPPPPPPVIP PTENEHDEHD ENNAEASAEL SNEGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD ETKKTQNDVL HAENVKAGRD KYKTLRQIRQ GNTKQRIDEF EAM |
| 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条关于RDX重组蛋白的模拟参考文献示例(注：文献为模拟生成，非真实存在，仅供参考格式和内容框架)：
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1. **文献名称**: *Heterologous Expression and Characterization of RDX-Degrading Enzyme from Pseudomonas putida*
**作者**: Smith, J.R.; Johnson, A.B.; Lee, C.
**摘要**: 本研究克隆了来自*Pseudomonas putida*的RDX降解基因*rdxA*，并在大肠杆菌中成功表达重组蛋白。通过体外活性实验证实，该重组酶能在厌氧条件下高效催化RDX分解为亚硝基衍生物，为生物修复RDX污染提供了潜在工具。
2. **文献名称**: *Engineering a Thermostable RDX Hydrolase for Environmental Remediation*
**作者**: Zhang, Y.; Wang, H.; Patel, R.
**摘要**: 通过定向进化技术优化天然RDX水解酶，获得热稳定性增强的重组蛋白。该酶在50℃下仍保持80%活性，并可降解土壤中90%的RDX污染物，为高温环境下的爆炸物降解提供了新策略。
3. **文献名称**: *Mechanistic Insights into RDX Degradation by a Recombinant Cytochrome P450 System*
**作者**: Gupta, S.; Thompson, M.K.; Fernández, L.
**摘要**: 解析了重组细胞色素P450酶与RDX的分子相互作用机制，发现其依赖NADPH的氧化还原途径将RDX转化为无毒的甲酸和氮气。通过晶体结构分析揭示了活性位点的关键氨基酸残基。
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如需真实文献，建议在PubMed、Web of Science等数据库检索关键词：**RDX degradation**、**recombinant enzyme**、**bioremediation**。部分相关领域真实作者包括：Jugder B.-E., Hawari J., Bhushan B. 等。
RDX recombinant protein, derived from the Rhodococcus genus of bacteria, is a engineered protein designed for enhanced catalytic efficiency in degrading nitro-organic compounds, particularly the explosive contaminant RDX (hexahydro-1.3.5-trinitro-1.3.5-triazine). Naturally occurring Rhodococcus strains exhibit limited RDX degradation capabilities through cytochrome P450 enzymes. However, recombinant DNA technology has enabled the optimization of these enzymes by cloning, modifying, and overexpressing target genes in heterologous hosts like E. coli or yeast.
The recombinant RDX protein typically retains the core structural domains responsible for substrate binding and redox reactions while incorporating modifications to improve stability, solubility, and activity under diverse environmental conditions. Advanced protein engineering strategies, including site-directed mutagenesis and fusion tags, are employed to address challenges such as enzyme inactivation by RDX breakdown intermediates.
Applications span environmental bioremediation and biosensing. In contaminated soils and groundwater, the recombinant protein accelerates RDX breakdown into non-toxic metabolites like nitrous oxide and formaldehyde. Its thermostable variants show promise in ex-situ treatment systems. Additionally, RDX-specific binding properties enable its integration into biosensors for detecting explosive residues in military zones or industrial waste.
Ongoing research focuses on multi-enzyme cascades and immobilization techniques to enhance operational stability. Compatibility with synthetic biology frameworks also positions it as a modular component for engineered microbial consortia. Despite progress, challenges remain in scaling production cost-effectively and ensuring long-term enzymatic activity in complex matrices. The development of RDX recombinant protein exemplifies how synthetic biology bridges microbial metabolism with anthropogenic pollutant management needs.
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