| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Selenot |
| Uniprot No | P62341 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-195aa |
| 氨基酸序列 | S ANLGGVPSKR LKMQYATGPL LKFQICVSUG YRRVFEEYMR VISQRYPDIR IEGENYLPQP IYRHIASFLS VFKLVLIGLI IVGKDPFAFF GMQAPSIWQW GQENKVYACM MVFFLSNMIE NQCMSTGAFE ITLNDVPVWS KLESGHLPSM QQLVQILDNE MKLNVHMDSI PHHRS |
| 预测分子量 | 22,3 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Selenot(硒蛋白T，Selenoprotein T)重组蛋白研究的模拟参考文献示例(文献信息为虚构，仅供参考)：
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1. **文献名称**：Crystal structure of recombinant human Selenoprotein T reveals redox-active motifs
**作者**：Smith A, et al.
**摘要**：通过X射线晶体学解析了重组人源Selenot蛋白的三维结构，揭示了其保守的硫氧还蛋白样折叠模式及CXXU(U为硒代半胱氨酸)活性位点，提示其在细胞氧化还原调控中的潜在作用。
2. **文献名称**：Recombinant Selenoprotein T modulates ER stress in neuronal cells
**作者**：Lee JH, et al.
**摘要**：研究利用大肠杆菌表达的重组Selenot蛋白，发现其通过调节内质网(ER)应激反应通路(如IRE1α-XBP1)减轻神经元细胞氧化损伤，为神经退行性疾病治疗提供新靶点。
3. **文献名称**：Functional characterization of recombinant Selenoprotein T in pancreatic β-cell survival
**作者**：Garcia-Ruiz C, et al.
**摘要**：通过重组Selenot蛋白的体外功能实验，证明其通过激活Ca²⁺依赖性信号通路促进胰岛β细胞存活，可能参与糖尿病病理过程的调控。
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**注意**：以上文献为模拟生成，实际研究中请通过PubMed、Google Scholar等平台检索真实文献(关键词：Selenoprotein T, recombinant, structure/function)。真实文献可能涉及重组表达系统(如原核/真核表达)、疾病模型中的功能验证等方向。
Selenoprotein T (Selenot), a member of the selenoprotein family, is a thioredoxin-like enzyme characterized by the presence of selenium in the form of selenocysteine (Sec) at its active site. Encoded by the SELENOT gene, it is ubiquitously expressed in mammalian tissues, with notable roles in redox regulation, calcium homeostasis, and cellular stress responses. Selenot's structure includes a conserved CXXU motif (U representing Sec), enabling its participation in disulfide bond reduction and oxidative protein folding within the endoplasmic reticulum (ER).
Research highlights Selenot's involvement in neuroprotection, hormone secretion, and embryonic development. Its dysregulation has been linked to neurodegenerative diseases, metabolic disorders, and cancer. However, studying native Selenot is challenging due to the technical complexity of incorporating Sec—a non-canonical amino acid requiring a specific tRNA and translational recoding mechanism. Recombinant Selenot production addresses this by employing engineered expression systems (e.g., E. coli or mammalian cells) with optimized Sec insertion elements. These systems enable large-scale synthesis of functional Selenot for structural studies, enzymatic activity assays, and therapeutic exploration.
Recent advances focus on modifying recombinant Selenot for enhanced stability or targeted delivery, particularly in contexts like ER stress-related pathologies. Its unique redox properties and tissue-specific expression make it a promising candidate for biomarker development or redox-based therapies. Ongoing studies aim to unravel its precise molecular interactions and validate its therapeutic potential in preclinical models.
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