| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ESD |
| Uniprot No | P10768 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-282aa |
| 氨基酸序列 | MALKQISSNK CFGGLQKVFE HDSVELNCKM KFAVYLPPKA ETGKCPALYW LSGLTCTEQN FISKSGYHQS ASEHGLVVIA PDTSPRGCNI KGEDESWDFG TGAGFYVDAT EDPWKTNYRM YSYVTEELPQ LINANFPVDP QRMSIFGHSM GGHGALICAL KNPGKYKSVS AFAPICNPVL CPWGKKAFSG YLGTDQSKWK AYDATHLVKS YPGSQLDILI DQGKDDQFLL DGQLLPDNFI AACTEKKIPV VFRLQEGYDH SYYFIATFIT DHIRHHAKYL NA |
| 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. |
以下是关于ESD(酯酶D)重组蛋白的参考文献示例(注：文献信息为示例性内容，实际引用请核实原文)：
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1. **文献名称**: *Expression and Purification of Recombinant Human Esterase D for Functional Analysis*
**作者**: Zhang, L., Wang, Y., & Chen, H.
**摘要**: 本研究报道了在大肠杆菌中高效表达人源重组酯酶D(ESD)的方法，通过His标签纯化获得高纯度蛋白。酶活性实验表明，重组ESD对特定酯类底物具有显著水解活性，为后续酶学机制研究奠定了基础。
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2. **文献名称**: *Crystal Structure of Recombinant Esterase D from *Saccharomyces cerevisiae*: Insights into Substrate Specificity*
**作者**: Tanaka, K., et al.
**摘要**: 通过X射线晶体学解析了酵母来源重组ESD的三维结构，揭示了其催化三联体(Ser-His-Asp)的构象及底物结合口袋特征。结构分析为设计ESD突变体以优化工业酯类水解应用提供了依据。
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3. **文献名称**: *Clinical Application of Recombinant ESD as a Biomarker in Liver Disease Diagnosis*
**作者**: Gupta, S., et al.
**摘要**: 研究评估了重组ESD蛋白在肝病患者血清中的表达水平，发现其活性与肝纤维化程度显著相关。重组ESD被证明可作为潜在的非侵入性诊断标志物。
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4. **文献名称**: *Enhancing Thermostability of Recombinant Esterase D via Directed Evolution*
**作者**: Müller, J., & Schmidt-Dannert, C.
**摘要**: 利用定向进化技术改造重组ESD，获得热稳定性提升的突变体。突变体在60℃下保留80%活性，适用于高温工业催化环境。
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**注**：以上文献为模拟内容，实际研究中请通过数据库(如PubMed、Web of Science)检索真实文献。若需具体领域文献，建议补充ESD的研究方向(如疾病机制、工业酶工程等)。
**Background of ESD Recombinant Proteins**
ESD (S-formylglutathione hydrolase), also known as esterase D, is a critical enzyme involved in cellular detoxification pathways, particularly in the breakdown of formaldehyde and S-formylglutathione. This enzyme plays a role in the glutathione-dependent formaldehyde oxidation pathway, which is essential for mitigating the toxic effects of endogenous or exogenous aldehydes. The ESD gene, located on human chromosome 13. has garnered attention due to its association with various physiological processes and potential implications in disease mechanisms, including oxidative stress-related disorders and alcohol metabolism.
Recombinant ESD proteins are engineered using genetic engineering techniques, where the ESD gene is cloned into expression vectors and produced in host systems like *E. coli*, yeast, or mammalian cells. This approach enables large-scale, high-purity production of the protein for functional and structural studies. Recombinant technology allows researchers to modify or tag the protein, facilitating applications such as enzyme activity assays, antibody development, and interaction studies with substrates or inhibitors.
The development of ESD recombinant proteins has advanced research in understanding its catalytic mechanism, substrate specificity, and role in cellular redox homeostasis. Additionally, these proteins are valuable tools in drug discovery, particularly for designing inhibitors targeting aldehyde metabolism pathways in conditions like alcohol-induced organ damage or cancer. Structural studies using recombinant ESD have also provided insights into its active site architecture, aiding in the rational design of therapeutic molecules.
Overall, ESD recombinant proteins serve as indispensable resources in both basic research and translational applications, bridging gaps between biochemical characterization and clinical relevance in metabolic and degenerative diseases.
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