| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | oxyR |
| Uniprot No | P0ACQ4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-305aa |
| 氨基酸序列 | MNIRDLEYLVALAEHRHFRRAADSCHVSQPTLSGQIRKLEDELGVMLLERTSRKVLFTQAGMLLVDQARTVLREVKVLKEMASQQGETMSGPLHIGLIPTVGPYLLPHIIPMLHQTFPKLEMYLHEAQTHQLLAQLDSGKLDCVILALVKESEAFIEVPLFDEPMLLAIYEDHPWANRECVPMADLAGEKLLMLEDGHCLRDQAMGFCFEAGADEDTHFRATSLETLRNMVAAGSGITLLPALAVPPERKRDGVVYLPCIKPEPRRTIGLVYRPGSPLRSRYEQLAEAIRARMDGHFDKVLKQAV |
| 预测分子量 | 82.1 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. |
以下是关于 **oxyR重组蛋白** 的3篇参考文献概要：
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1. **文献名称**：*Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation*
**作者**：Toledano, M.B., et al.
**摘要**：该研究解析了OxyR蛋白通过氧化还原敏感的二硫键形成，从还原态(非活性)转变为氧化态(活性)的结构机制，揭示了其作为氧化应激反应转录因子的分子开关作用。
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2. **文献名称**：*Structural basis of redox-dependent activation of the OxyR transcription factor*
**作者**：Jo, I., et al.
**摘要**：通过X射线晶体学分析重组OxyR蛋白的氧化态和还原态结构，阐明了其构象变化如何调控DNA结合能力，并驱动抗氧化基因的转录激活。
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3. **文献名称**：*The OxyR regulon: A model for bacterial oxidative stress response regulation*
**作者**：Christman, M.F., et al.
**摘要**：早期研究利用重组OxyR蛋白验证其作为全局调控因子的功能，证明其在过氧化氢应激下直接激活多个抗氧化基因(如katG、ahpCF)的表达。
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4. **文献名称**：*Purification and functional analysis of recombinant OxyR protein from Escherichia coli*
**作者**：Zheng, M., et al.
**摘要**：报道了重组OxyR蛋白的高效表达与纯化方法，并通过体外实验证实其特异性结合靶DNA序列的能力依赖于氧化还原状态的变化。
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这些文献涵盖了OxyR的结构、功能机制及重组蛋白的应用研究，为理解细菌氧化应激应答提供了关键依据。
The OxyR protein is a key transcriptional regulator in bacteria, primarily known for its role in oxidative stress response. Belonging to the LysR family of transcription factors, OxyR acts as a redox sensor that detects hydrogen peroxide (H₂O₂) and activates antioxidant defense mechanisms. In its reduced state, OxyR remains inactive, but upon oxidation by H₂O₂, it undergoes a structural rearrangement, forming an intramolecular disulfide bond. This conformational change enables OxyR to bind promoter regions of target genes, such as *katG* (encoding catalase) and *ahpCF* (alkyl hydroperoxide reductase), initiating their transcription to neutralize reactive oxygen species (ROS).
Recombinant OxyR proteins are engineered for in vitro studies to dissect its regulatory mechanisms and redox-sensing properties. Typically produced in *E. coli* expression systems, these proteins retain the ability to dimerize and interact with DNA, mimicking native behavior. Structural studies using recombinant OxyR have revealed critical domains involved in redox sensing, DNA binding, and co-activator interactions, providing insights into its allosteric activation.
Research on OxyR has implications for understanding bacterial adaptation to host immune defenses, as oxidative stress responses are crucial for pathogen survival during infections. Additionally, recombinant OxyR serves as a tool for developing antimicrobial strategies targeting redox signaling pathways. Its conserved function across diverse bacterial species, including *Salmonella* and *Pseudomonas*, underscores its broad relevance in microbiology and infectious disease research. Recent advances also explore engineered OxyR variants for synthetic biology applications, such as biosensors for oxidative stress or gene expression control systems.
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