| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSSG |
| Uniprot No | P36269 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-586aa |
| 氨基酸序列 | MARGYGATVSLVLLGLGLALAVIVLAVVLSRHQAPCGPQAFAHAAVAADSKVCSDIGRAILQQQGSPVDATIAALVCTSVVNPQSMGLGGGVIFTIYNVTTGKVEVINARETVPASHAPSLLDQCAQALPLGTGAQWIGVPGELRGYAEAHRRHGRLPWAQLFQPTIALLRGGHVVAPVLSRFLHNSILRPSLQASTLRQLFFNGTEPLRPQDPLPWPALATTLETVATEGVEVFYTGRLGQMLVEDIAKEGSQLTLQDLAKFQPEVVDALEVPLGDYTLYSPPPPAGGAILSFILNVLRGFNFSTESMARPEGRVNVYHHLVETLKFAKGQRWRLGDPRSHPKLQNASRDLLGETLAQLIRQQIDGRGDHQLSHYSLAEAWGHGTGTSHVSVLGEDGSAVAATSTINTPFGAMVYSPRTGIILNNELLDLCERCPRGSGTTPSPVSGDRVGGAPGRCWPPVPGERSPSSMVPSILINKAQGSKLVIGGAGGELIISAVAQAIMSKLWLGFDLRAAIAAPILHVNSKGCVEYEPNFSQEVQRGLQDRGQNQTQRPFFLNVVQAVSQEGACVYAVSDLRKSGEAAGY |
| 预测分子量 | 62,2 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篇涉及GSSG(氧化型谷胱甘肽)与重组蛋白相关研究的文献摘要概括：
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1. **文献名称**：*Optimization of Glutathione Disulfide (GSSG) Delivery in Recombinant Protein Refolding*
**作者**：Kim, J.H. et al.
**摘要**：研究通过调控氧化还原缓冲体系(含GSSG/GSH)优化包涵体重组蛋白复性效率，发现GSSG浓度梯度对蛋白质正确二硫键形成具有剂量依赖性，并建立了数学模型预测最佳复性条件。
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2. **文献名称**：*Role of Oxidized Glutathione in Stabilizing Therapeutic Antibody Structure*
**作者**：Zhang, L. & Wang, Q.
**摘要**：探讨GSSG在单克隆抗体生产工艺中的稳定性作用，证明添加GSSG可减少抗体聚集现象，通过质谱分析证实其通过维持特定巯基氧化态提升蛋白热稳定性。
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3. **文献名称**：*In vivo Analysis of GSSG-Regulated Protein Folding in E. coli*
**作者**：Mendez, R. et al.
**摘要**：利用大肠杆菌表达系统，研究胞内GSSG/GSH比例对重组酶活性恢复的影响，发现提高GSSG水平可纠正错误折叠蛋白，并通过荧光标记实时监测折叠过程。
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注：以上为示例性概括，实际文献需通过学术数据库(如PubMed、Web of Science)检索具体标题及作者。如需真实文献，建议使用关键词“GSSG recombinant protein folding”或“glutathione disulfide protein engineering”进一步查询。
**Background of Recombinant GSSG Protein**
Glutathione disulfide (GSSG), the oxidized form of glutathione, is a critical molecule in cellular redox homeostasis. Glutathione, a tripeptide (γ-glutamyl-cysteinyl-glycine), exists in two states: reduced (GSH) and oxidized (GSSG). GSH serves as a primary antioxidant, neutralizing reactive oxygen species (ROS) and maintaining cellular redox balance. During oxidative stress, GSH donates electrons to oxidants, converting to GSSG, which is later recycled back to GSH by glutathione reductase (GR) using NADPH. The GSH/GSSG ratio is a key indicator of cellular oxidative status.
Recombinant GSSG-related proteins, such as glutathione reductase or glutathione peroxidase, are engineered using genetic modification techniques. These proteins are produced by inserting target genes into expression systems (e.g., *E. coli*, yeast, or mammalian cells), followed by purification. Recombinant technology ensures high purity, scalability, and consistency, addressing challenges in studying native proteins, which are often low in abundance or difficult to isolate.
Applications of recombinant GSSG-associated proteins span research, therapeutics, and industry. In biomedicine, they aid in studying oxidative stress mechanisms in diseases like cancer, neurodegeneration, and aging. Recombinant GR or peroxidases are explored as therapeutic agents or drug targets. Industrially, they enhance antioxidant capacity in biologics production or serve as tools in diagnostics.
Furthermore, recombinant GSSG itself (though a small molecule) is synthesized for experimental use, such as inducing oxidative stress in models. Overall, recombinant GSSG-related proteins advance our understanding of redox biology and offer tailored solutions for health and biotechnology challenges.
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