| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | gshA |
| 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 | MIPDVSQALAWLEKHPQALKGIQRGLERETLRVNADGTLATTGHPEALGSALTHKWITTDFAEALLEFITPVDGDIEHMLTFMRDLHRYTARNMGDERMWPLSMPCYIAEGQDIELAQYGTSNTGRFKTLYREGLKNRYGALMQTISGVHYNFSLPMAFWQAKCGDISGADAKEKISAGYFRVIRNYYRFGWVIPYLFGASPAICSSFLQGKPTSLPFEKTECGMYYLPYATSLRLSDLGYTNKSQSNLGITFNDLYEYVAGLKQAIKTPSEEYAKIGIEKDGKRLQINSNVLQIENELYAPIRPKRVTRSGESPSDALLRGGIEYIEVRSLDINPFSPIGVDEQQVRFLDLFMVWCALADAPEMSSSELACTRVNWNRVILEGRKPGLTLGIGCETAQFPLPQVGKDLFRDLKRVAQTLDSINGGEAYQKVCDELVACFDNPDLTFSARILRSMIDTGIGGTGKAFAEAYRNLLREEPLEILREEDFVAEREASERRQQEMEAADTEPFAVWLEKHA |
| 预测分子量 | 74.3 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篇关于gshA重组蛋白研究的模拟参考文献(基于常见研究方向构建，实际文献请通过学术数据库查询)：
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1. **文献名称**：*Heterologous expression and characterization of γ-glutamylcysteine synthetase (gshA) from Escherichia coli in Pichia pastoris*
**作者**：Zhang L, et al.
**摘要**：本研究在毕赤酵母中成功表达了重组gshA蛋白，优化了诱导条件(如甲醇浓度、pH)以提高酶活性。纯化的重组酶显示出比原核表达更高的热稳定性和催化效率，为工业化生产谷胱甘肽提供了新策略。
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2. **文献名称**：*Enhancing glutathione production by engineered overexpression of gshA in Corynebacterium glutamicum*
**作者**：Wang Y, et al.
**摘要**：通过在大肠杆菌中重组表达谷氨酸棒状杆菌的gshA基因，构建高效谷胱甘肽合成工程菌。通过启动子优化和金属离子(Mg²⁺)调控，使胞内γ-GCS酶活提高3倍，谷胱甘肽产量达到15.2 g/L。
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3. **文献名称**：*Crystal structure and functional analysis of recombinant gshA from Pseudomonas aeruginosa*
**作者**：Tanaka K, et al.
**摘要**：首次解析了铜绿假单胞菌gshA重组蛋白的晶体结构(2.1 Å)，揭示其ATP结合域和底物结合位点的关键残基。突变实验证实Asp102和Arg245对γ-谷氨酰半胱氨酸合成至关重要，为开发靶向抑制剂奠定基础。
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**建议**：实际文献可通过PubMed或Web of Science搜索关键词 "*gshA recombinant protein*" 或 "*γ-glutamylcysteine synthetase heterologous expression*"，并筛选近5-10年的高被引论文。
**Background of gshA Recombinant Protein**
The *gshA* gene encodes γ-glutamylcysteine synthetase (γ-GCS), a rate-limiting enzyme in the biosynthesis of glutathione (GSH), a critical tripeptide antioxidant found in most organisms. GSH plays essential roles in redox homeostasis, detoxification, and cellular defense against oxidative stress. Recombinant gshA protein is engineered through genetic engineering techniques, where the *gshA* gene is cloned into expression vectors and produced in heterologous host systems like *E. coli*, yeast, or mammalian cells. This approach enables large-scale production of the enzyme for research and industrial applications.
Studying recombinant gshA protein provides insights into GSH metabolism and its regulatory mechanisms, which are linked to diseases such as neurodegenerative disorders, cancer, and aging. Researchers utilize recombinant gshA to investigate enzyme kinetics, substrate specificity, and inhibition, aiding drug development targeting GSH-deficient conditions. Additionally, it serves as a tool in biotechnological applications, including biofortification of crops with enhanced stress tolerance and microbial production of GSH for nutraceuticals.
Challenges in producing functional gshA recombinant protein include maintaining its enzymatic activity post-purification and optimizing expression conditions due to its susceptibility to oxidative inactivation. Recent advances in protein engineering and expression systems have improved stability and yield, facilitating broader use in both basic and applied research. Overall, gshA recombinant protein remains a vital resource for understanding cellular antioxidant systems and developing therapeutic or industrial solutions tied to oxidative stress management.
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