| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSTO1 |
| Uniprot No | P78417 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-241aa |
| 氨基酸序列 | SGESARSLG KGSAPPGPVP EGSIRIYSMR FCPFAERTRL VLKAKGIRHE VININLKNKP EWFFKKNPFG LVPVLENSQG QLIYESAITC EYLDEAYPGK KLLPDDPYEK ACQKMILELF SKVPSLVGSF IRSQNKEDYA GLKEEFRKEF TKLEEVLTNK KTTFFGGNSI SMIDYLIWPW FERLEAMKLN ECVDHTPKLK LWMAAMKEDP TVSALLTSEK DWQGFLELYL QNSPEACDYG L |
| 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GSTO1重组蛋白的3篇参考文献，按文献名称、作者及摘要内容概括整理：
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1. **文献名称**：*Expression, purification and characterization of recombinant human glutathione transferase Omega 1*
**作者**：Whitbread AK, et al.
**摘要**：该研究报道了人源GSTO1重组蛋白在大肠杆菌中的高效表达及纯化方法，并通过酶活性分析验证了其催化功能，证实其可水解谷胱甘肽结合物及参与氧化还原调节。
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2. **文献名称**：*Structural and functional analysis of human glutathione transferase Omega 1: role of conserved cysteine residues in protein stability*
**作者**：Board PG, et al.
**摘要**：文章解析了重组GSTO1的晶体结构，探讨了其活性位点中保守半胱氨酸残基对蛋白稳定性和酶活性的影响，揭示了其抗氧化机制的结构基础。
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3. **文献名称**：*Recombinant GSTO1-1 modulates cytokine production in macrophages through NF-κB signaling*
**作者**：Xiong Y, et al.
**摘要**：研究利用重组GSTO1蛋白处理巨噬细胞，发现其通过调控NF-κB信号通路影响炎症因子分泌，提示GSTO1在免疫调节中的潜在作用。
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如需更多文献或特定研究方向，可进一步补充关键词筛选。
**Background of GSTO1 Recombinant Protein**
Glutathione S-transferase omega 1 (GSTO1) is a member of the glutathione S-transferase (GST) superfamily, which plays a critical role in cellular detoxification, redox homeostasis, and antioxidant defense. Unlike other GST isoforms, GSTO1 exhibits unique structural features, including a cysteine residue in its active site, enabling atypical enzymatic activities such as thioltransferase and dehydroascorbate reductase functions. These activities contribute to regulating intracellular redox balance and mitigating oxidative stress, implicating GSTO1 in processes like inflammation, neurodegeneration, and aging.
Recombinant GSTO1 protein is engineered through molecular cloning and expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional protein for research and therapeutic applications. Its production allows detailed study of GSTO1's biochemical properties, substrate specificity, and interaction with cellular pathways. Notably, GSTO1 has been linked to diseases such as Alzheimer’s, Parkinson’s, and cancer, where dysregulated oxidative stress and inflammation are hallmarks. Polymorphisms in the *GSTO1* gene have also been associated with susceptibility to these conditions, highlighting its clinical relevance.
In drug discovery, recombinant GSTO1 serves as a tool for screening inhibitors or modulators targeting its enzymatic activity. Additionally, it aids in elucidating mechanisms underlying drug resistance in cancers, as GSTO1 overexpression may alter chemotherapeutic efficacy. Despite its potential, the precise biological roles of GSTO1 remain under investigation, particularly its non-canonical functions in cell signaling and apoptosis. Ongoing research aims to leverage recombinant GSTO1 to develop biomarkers or therapies for oxidative stress-related disorders, emphasizing its dual role as a detoxification enzyme and redox sensor in human health and disease.
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