| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSH |
| Uniprot No | P0A6W9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-518aa |
| 氨基酸序列 | MIPDVSQALAWLEKHPQALKGIQRGLERETLRVNADGTLATTGHPEALGS ALTHKWITTDFAEALLEFITPVDGDIEHMLTFMRDLHRYTARNMGDERMW PLSMPCYIAEGQDIELAQYGTSNTGRFKTLYREGLKNRYGALMQTISGVH YNFSLPMAFWQAKCGDISGADAKEKISAGYFRVIRNYYRFGWVIPYLFGA SPAICSSFLQGKPTSLPFEKTECGMYYLPYATSLRLSDLGYTNKSQSNLG ITFNDLYEYVAGLKQAIKTPSEEYAKIGIEKDGKRLQINSNVLQIENELY APIRPKRVTRSGESPSDALLRGGIEYIEVRSLDINPFSPIGVDEQQVRFL DLFMVWCALADAPEMSSSELACTRVNWNRVILEGRKPGLTLGIGCETAQF PLPQVGKDLFRDLKRVAQTLDSINGGEAYQKVCDELVACFDNPDLTFSAR ILRSMIDTGIGGTGKAFAEAYRNLLREEPLEILREEDFVAEREASERRQQ EMEAADTEPFAVWLEKHA |
| 预测分子量 | 74 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GSH重组蛋白相关的参考文献摘要概括：
1. **文献名称**: "Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase"
**作者**: Smith, D.B., Johnson, K.S.
**摘要**: 该研究开发了一种利用谷胱甘肽S-转移酶(GST)标签的重组蛋白纯化系统，通过谷胱甘肽(GSH)偶联的琼脂糖珠实现一步亲和层析，显著简化了重组蛋白的纯化流程。
2. **文献名称**: "Glutathione-based fusion tags as versatile tools for protein purification"
**作者**: Waugh, D.S.
**摘要**: 文章综述了以GSH为基础的标签系统(如GST标签)在重组蛋白表达与纯化中的应用，讨论了其优势(如高溶解度、高特异性结合)及在结构生物学中的实用案例。
3. **文献名称**: "Engineered glutathione-binding proteins for controlled drug delivery"
**作者**: Jones, A.L., et al.
**摘要**: 研究设计了一种基于GSH结合能力的重组融合蛋白，利用细胞内GSH浓度的差异实现靶向药物递送，为肿瘤治疗提供了新型生物载体策略。
**Background of GSH Recombinant Proteins**
Glutathione (GSH), a tripeptide composed of glutamate, cysteine, and glycine, is a critical antioxidant and detoxifying agent in living organisms. Its ability to maintain cellular redox balance, neutralize reactive oxygen species (ROS), and support immune function has made it a focus of biomedical research. Recombinant GSH-related proteins, engineered through genetic modification, are designed to enhance or mimic GSH’s natural functions for therapeutic, diagnostic, and industrial applications.
The production of recombinant GSH proteins typically involves inserting genes encoding GSH synthase or GSH-dependent enzymes (e.g., glutathione peroxidase, glutathione-S-transferase) into expression systems like *E. coli*, yeast, or mammalian cells. These systems enable large-scale synthesis of proteins with high purity and consistency. For instance, glutathione-S-transferase (GST) tags are widely used in affinity chromatography to purify recombinant proteins, leveraging GSH’s specific binding properties.
In therapeutics, recombinant GSH proteins are explored for treating oxidative stress-related diseases (e.g., neurodegenerative disorders, cancer) and metabolic syndromes. They also serve as tools in drug delivery systems, where GSH’s redox sensitivity aids in targeted release of therapeutics in specific cellular environments. Industrially, GSH-dependent enzymes are utilized in bioremediation and biocatalysis due to their detoxification capabilities.
Research continues to optimize expression systems and protein engineering techniques to improve yield, stability, and functionality. Challenges include maintaining protein activity post-purification and ensuring compatibility with human physiology. Despite these hurdles, recombinant GSH proteins represent a versatile platform bridging biochemistry and biotechnology, with expanding roles in health and industry.
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