| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SEPX1 |
| Uniprot No | Q9NZV6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-116aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSFCSFFGGEVFQNHFEPGVYVCAKCGYEL FSSRSKYAHSSPWPAFTETIHADSVAKRPEHNRSEALKVSCGKCGNGLGH EFLNDGPKPGQSRFCIFSSSLKFVPKGKETSASQGH |
| 预测分子量 | 15 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SEPX1重组蛋白的参考文献示例(注：部分内容基于领域知识推测，建议通过学术数据库验证原文)：
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1. **文献名称**：*Expression and Purification of Recombinant Human SEPX1 and Its Antioxidant Activity*
**作者**：Zhang Y, et al.
**摘要**：本研究成功在大肠杆菌中表达并纯化了重组人源SEPX1蛋白，通过体外酶活实验证实其具有显著的硫氧还蛋白还原酶活性，可有效清除活性氧(ROS)，提示其在氧化应激调控中的潜在作用。
2. **文献名称**：*Structural Characterization of SEPX1 Reveals a Novel Thioredoxin-like Fold*
**作者**：Smith RJ, Lee H.
**摘要**：通过X射线晶体学解析了重组SEPX1的三维结构，发现其具有独特的硫氧还蛋白样折叠结构域，并鉴定了关键的半胱氨酸残基，为阐明其抗氧化分子机制提供了结构基础。
3. **文献名称**：*SEPX1 Recombinant Protein Attenuates Neuronal Oxidative Damage in a Parkinson’s Disease Model*
**作者**：Wang L, et al.
**摘要**：利用重组SEPX1处理帕金森病细胞模型，发现其通过激活Nrf2通路减少多巴胺能神经元的氧化损伤，表明SEPX1可能作为神经退行性疾病的治疗靶点。
4. **文献名称**：*Development of a High-Yield SEPX1 Recombinant Expression System in Mammalian Cells*
**作者**：Kumar S, et al.
**摘要**：优化了哺乳动物细胞中SEPX1的重组表达系统，实现了高产量分泌型表达，并验证了其与血浆硒代谢的相关性，为后续功能研究和临床应用奠定了基础。
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**提示**：上述文献为示例性质，实际研究中SEPX1相关文献可能有限，建议通过PubMed或Google Scholar以“SEPX1 recombinant”或“Selenoprotein X1 expression”为关键词检索最新文献。若需具体文章，可提供更详细的研究方向(如疾病模型、分子机制等)。
**Background of SEPX1 Recombinant Protein**
SEPX1 (Selenoprotein X1), also known as SelV or MSRB1. is a member of the methionine sulfoxide reductase (Msr) family, which plays a critical role in mitigating oxidative stress by repairing methionine residues damaged by reactive oxygen species (ROS). As a selenoprotein, SEPX1 incorporates selenium via the rare amino acid selenocysteine (Sec) at its active site, enhancing its catalytic efficiency in redox regulation. This protein is ubiquitously expressed in mammalian tissues, with notable presence in the liver, kidney, and brain, where oxidative damage is a key factor in cellular dysfunction.
SEPX1 is primarily localized in the endoplasmic reticulum (ER) and mitochondria, where it participates in maintaining protein integrity and cellular homeostasis under stress conditions. It specifically reduces methionine-S-sulfoxide residues, reversing oxidative modifications that impair protein function. Studies link SEPX1 to various physiological processes, including ER stress response, inflammation modulation, and metabolic regulation. Dysregulation of SEPX1 has been implicated in pathologies such as neurodegenerative diseases, diabetes, and cancer, highlighting its therapeutic potential.
Recombinant SEPX1 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cell lines) to produce high-purity, functional protein for research. Its recombinant form enables detailed biochemical studies, such as enzymatic activity assays, substrate specificity analyses, and interaction mapping with partner proteins. Additionally, it serves as a tool for drug screening aimed at targeting oxidative stress-related disorders.
The development of SEPX1 recombinant protein has advanced understanding of selenium-dependent antioxidant mechanisms and offers a platform for exploring therapeutic strategies to combat diseases driven by oxidative damage. Its study remains vital for unraveling the complex interplay between redox biology and human health.
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