| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SELENOM |
| Uniprot No | Q8WWX9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-145aa |
| 氨基酸序列 | ATAYRPDWNRLSGLTRARVETCGGSQLNRLKEVKAFVTQDIPFYHNLVMKHLPGADPELVLLGRRYEELERIPLSEMTREEINALVQELGFYRKAAPDAQVPPEYVWAPAKPPEETSDHADL |
| 预测分子量 | 13.9kDa |
| 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SELENOM(Selenoprotein M)重组蛋白的3篇代表性文献摘要(基于近年研究趋势模拟，具体文献需核实)：
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1. **文献名称**：*"Recombinant human Selenoprotein M suppresses oxidative stress in neuronal cells via thioredoxin system"*
**作者**：Zhang Y, et al.
**摘要**：研究利用大肠杆菌重组表达人源SELENOM蛋白，验证其通过调节硫氧还蛋白系统减轻神经元氧化损伤的功能，表明其在神经退行性疾病中的潜在应用。
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2. **文献名称**：*"Structural characterization of Selenoprotein M and its interaction with amyloid-beta peptides"*
**作者**：Kurokawa S, et al.
**摘要**：通过重组表达获得高纯度SELENOM蛋白，解析其晶体结构并发现其与β淀粉样蛋白(Aβ)的结合能力，提示其可能在阿尔茨海默病中调节Aβ毒性。
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3. **文献名称**：*"Selenoprotein M knockout exacerbates hepatic ER stress: Rescue by recombinant protein delivery"*
**作者**：Li H, et al.
**摘要**：利用哺乳动物细胞系统表达重组SELENOM，证明其通过抑制内质网应激改善肝细胞损伤，为代谢性疾病治疗提供新靶点。
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注：以上为模拟文献摘要，实际研究需参考PubMed或Web of Science数据库(关键词：Selenoprotein M, recombinant expression, oxidative stress)。
SELENOM (Selenoprotein M) is a member of the selenoprotein family, characterized by the incorporation of selenocysteine (Sec), a rare amino acid encoded by the UGA codon, which typically serves as a stop signal. This unique feature requires a specific RNA structure, the SECIS element, to enable Sec insertion during translation. SELENOM is predominantly expressed in the brain, endocrine tissues, and liver, and is localized to the endoplasmic reticulum (ER), where it participates in redox homeostasis and calcium signaling. Structurally, it contains a conserved thioredoxin-like fold, suggesting roles in antioxidant defense and protein folding regulation.
Research links SELENOM to neuroprotection, glucose metabolism, and aging. It interacts with proteins involved in ER stress response and may mitigate oxidative damage implicated in Alzheimer’s disease and Parkinson’s disease. Dysregulation of SELENOM has been observed in metabolic disorders, such as diabetes, and certain cancers, highlighting its potential as a therapeutic target or biomarker.
Recombinant SELENOM production faces challenges due to the complex Sec incorporation mechanism. Heterologous expression systems (e.g., E. coli, mammalian cells) are optimized with Sec-rich media and engineered vectors containing SECIS elements to ensure proper translation. Purification often involves affinity tags and stringent redox conditions to maintain protein stability. Recombinant SELENOM enables functional studies, antibody development, and high-throughput screening for drug discovery. Current research focuses on elucidating its precise molecular mechanisms and exploring its therapeutic applications in neurodegeneration and metabolic diseases. Advances in selenoprotein engineering may enhance its production efficiency, facilitating broader biomedical applications.
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