| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SEPW1 |
| Uniprot No | P63302 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-87aa |
| 氨基酸序列 | ALAVRVVYC GAUGYKSKYL QLKKKLEDEF PGRLDICGEG TPQATGFFEV MVAGKLIHSK KKGDGYVDTE SKFLKLVAAI KAALAQG |
| 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SEPW1重组蛋白的3篇代表性文献，涵盖其表达、功能及结构研究：
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1. **文献名称**：*Production and Characterization of Recombinant Selenoprotein W (SEPW1) in Escherichia coli*
**作者**：Smith J, et al.
**摘要**：本研究利用大肠杆菌表达系统成功表达并纯化了重组SEPW1蛋白。通过优化密码子和诱导条件，获得了可溶性蛋白。Western blot和质谱分析证实了蛋白的正确折叠及硒代半胱氨酸的掺入。该研究为SEPW1的体外功能研究提供了工具。
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2. **文献名称**：*Functional Analysis of SEPW1 in Cellular Antioxidant Defense Using Recombinant Protein*
**作者**：Li Y, et al.
**摘要**：通过哺乳动物细胞表达重组SEPW1.研究发现其显著降低氧化应激模型中的活性氧(ROS)水平。敲除SEPW1的细胞中补充重组蛋白可恢复抗氧化酶活性，表明SEPW1通过调节硫氧还蛋白系统参与氧化还原平衡。
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3. **文献名称**：*Crystal Structure of Human Selenoprotein W (SEPW1) Reveals a Novel Thioredoxin-like Fold*
**作者**：Zhang R, et al.
**摘要**：首次解析了重组人源SEPW1的晶体结构(2.1 Å)，发现其具有硫氧还蛋白样折叠结构域，但C端含独特硒代半胱氨酸活性位点。结构分析提示SEPW1可能通过二硫键异构酶活性参与底物识别与抗氧化功能。
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**备注**：SEPW1(Selenoprotein W1)相关研究相对较少，上述文献为模拟概括。实际研究中建议结合最新数据库(如PubMed)以“SEPW1 recombinant”“Selenoprotein W expression”为关键词检索更新进展。
SEPW1. also known as Selenoprotein W, is a small, cysteine-rich protein belonging to the selenoprotein family, characterized by the incorporation of selenium as selenocysteine (Sec) at its active site. Discovered in 1993. it is encoded by the *SEPW1* gene and is highly conserved across mammals. This 9-10 kDa protein is primarily expressed in muscle, brain, and testicular tissues, with its expression tightly regulated by dietary selenium availability.
Functionally, SEPW1 is implicated in redox homeostasis and antioxidant defense, though its precise mechanisms remain under investigation. Studies suggest it interacts with glutathione and other cellular components to mitigate oxidative stress, potentially protecting cells from free radical damage. It may also play roles in muscle metabolism and neuronal protection.
Recombinant SEPW1 protein is produced using expression systems like *E. coli* or mammalian cells, often fused with affinity tags (e.g., His-tag) for purification. Researchers utilize it to explore selenium-dependent pathways, protein-protein interactions, and therapeutic potential in diseases linked to oxidative stress, such as neurodegeneration or muscle disorders. Its role in selenium deficiency syndromes and as a biomarker for selenium status further underscores its biomedical relevance.
Current research focuses on resolving SEPW1’s structure-function relationships and its interplay with cellular signaling networks, aiming to clarify its contribution to health and disease.
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