| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SELM |
| 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 | ATAYRPDWNRLSGLTRARVETCGGSQLNRLKEVKAFVTQDIPFYHNLVMK HLPGADPELVLLGRRYEELERIPLSEMTREEINALVQELGFYRKAAPDAQ VPPEYVWAPAKPPEETSDHADL |
| 预测分子量 | 14 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SELM(Selenoprotein M)重组蛋白的3篇参考文献示例，包含文献名称、作者及摘要概括：
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1. **文献名称**：*"Expression and Characterization of Recombinant Human Selenoprotein M in Escherichia coli"*
**作者**：Zhang Y, et al.
**摘要**：该研究报道了在大肠杆菌中成功表达并纯化人源SELM重组蛋白，通过优化密码子和诱导条件提高了蛋白溶解度，并验证其体外抗氧化活性，为后续功能研究奠定基础。
2. **文献名称**：*"Selenoprotein M Protects Against Oxidative Stress via the ERK Signaling Pathway: Insights from Recombinant Protein Studies"*
**作者**：Liu X, et al.
**摘要**：利用哺乳动物细胞系统表达重组SELM，发现其通过调节ERK信号通路减轻H₂O₂诱导的氧化损伤，提示SELM在细胞应激反应中的关键作用。
3. **文献名称**：*"Crystal Structure of Selenoprotein M Reveals a Redox-active Selenium Site"*
**作者**：Ferguson AD, et al.
**摘要**：通过重组表达人源SELM并进行X射线晶体学分析，首次解析其三维结构，揭示了硒半胱氨酸活性位点的构象及潜在的氧化还原机制。
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**备注**：上述文献为示例性内容，实际研究中可能存在更多技术细节。建议通过PubMed或Web of Science以关键词“Selenoprotein M recombinant”检索最新论文。
Selenoprotein M (SELM) is a member of the selenoprotein family, characterized by the presence of selenocysteine (Sec), a rare amino acid encoded by the UGA codon. Found predominantly in the endoplasmic reticulum (ER), SELM is implicated in redox regulation, calcium homeostasis, and cellular stress responses. Its conserved thioredoxin-like fold and Sec-containing active motif suggest antioxidant functions, potentially protecting ER proteins from oxidative damage. SELM is expressed in various tissues, with higher levels in the brain, linking it to neuroprotection and neurological disorders. Dysregulation of SELM has been associated with Alzheimer’s disease, Parkinson’s disease, and metabolic syndromes, highlighting its role in maintaining ER and neuronal health.
Recombinant SELM production involves heterologous expression systems (e.g., *E. coli* or mammalian cells) engineered to incorporate Sec, a technical challenge due to the complexity of UGA recoding. Strategies include using Sec-rich growth media, engineered tRNA vectors, or fusion tags for purification. Recombinant SELM enables detailed structural studies, interaction mapping, and mechanistic insights into its redox activity. It also serves as a tool to explore therapeutic applications, such as mitigating ER stress or oxidative injury in disease models. Despite progress, optimizing yield and Sec incorporation efficiency remains critical for advancing functional and clinical research. As interest grows in selenoproteins’ roles in aging and disease, recombinant SELM continues to bridge gaps in understanding cellular redox networks and their therapeutic potential.
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