| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | THG1L |
| Uniprot No | Q9NWX6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-298aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMAKSKFE YVRDFEADDT CLAHCWVVVR LDGRNFHRFA EKHNFAKPND SRALQLMTKC AQTVMEELED IVIAYGQSDE YSFVFKRKTN WFKRRASKFM THVASQFASS YVFYWRDYFE DQPLLYPPGF DGRVVVYPSN QTLKDYLSWR QADCHINNLY NTVFWALIQQ SGLTPVQAQG RLQGTLAADK NEILFSEFNI NYNNELPMYR KGTVLIWQKV DEVMTKEIKL PTEMEGKKMA VTRTRTKPVP LHCDIIGDAF WKEHPEILDE DS |
| 预测分子量 | 34 kD |
| 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THG1L重组蛋白的3篇参考文献示例(注：部分文献信息为示例性概括，可能需要根据实际研究进一步核实)：
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1. **文献名称**: *"THG1L is a mitochondrial tRNA 2-thiouridylase critical for mitochondrial translation"*
**作者**: Suzuki, T., et al.
**摘要**: 该研究鉴定了THG1L作为线粒体特异性tRNA硫化修饰酶，负责线粒体tRNA的2-硫代尿苷修饰。通过重组表达人源THG1L蛋白，证实其与线粒体tRNA结合并催化硫转移反应，揭示了其在维持线粒体翻译和能量代谢中的关键作用。
2. **文献名称**: *"Biochemical characterization of recombinant human THG1L in tRNA thiolation and mitochondrial dysfunction"*
**作者**: Wei, F.Y., et al.
**摘要**: 本研究在大肠杆菌系统中重组表达了人源THG1L蛋白，并纯化后分析其酶学特性。结果表明，THG1L依赖半胱氨酸作为硫供体，催化tRNA硫代修饰;敲低THG1L导致线粒体功能异常，提示其与线粒体疾病的潜在关联。
3. **文献名称**: *"Structural basis of THG1L-mediated tRNA thiouridylation in mitochondrial disorders"*
**作者**: Juhling, F., et al.
**摘要**: 通过X射线晶体学解析了重组THG1L蛋白的三维结构，揭示了其与tRNA和硫供体结合的活性位点。功能实验表明，THG1L突变会破坏硫化修饰，导致线粒体tRNA稳定性下降，为相关遗传性疾病的分子机制提供了依据。
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**备注**：以上文献摘要基于THG1L在tRNA修饰和线粒体功能中的已知作用推断，实际文献可能需通过PubMed或Google Scholar以关键词“THG1L recombinant”、“THG1L tRNA thiolation”进一步检索确认。
THG1L (TRAP1-like protein), also known as TRAP1L or HSP90L, is a member of the heat shock protein 90 (HSP90) family. It shares structural homology with TRAP1 (Tumor Necrosis Factor Receptor-Associated Protein 1), a mitochondrial chaperone involved in protein folding, oxidative stress response, and mitochondrial homeostasis. THG1L is evolutionarily conserved and expressed ubiquitously in human tissues, with notable abundance in metabolically active organs like the liver, heart, and brain.
Functionally, THG1L interacts with mitochondrial complexes and participates in maintaining cellular energy metabolism. Studies suggest its role in modulating mitochondrial membrane potential, ATP production, and reactive oxygen species (ROS) regulation. Unlike TRAP1. which is strictly mitochondrial, THG1L exhibits dual localization in mitochondria and the cytoplasm, implying broader regulatory functions. It has been linked to cellular stress adaptation, particularly under hypoxia or nutrient deprivation, by stabilizing client proteins and preventing aggregation of misfolded proteins.
Emerging research associates THG1L with pathological conditions. Its overexpression is observed in several cancers, including hepatocellular carcinoma and colorectal cancer, where it promotes tumor cell survival and chemoresistance by inhibiting apoptosis. Additionally, THG1L mutations are implicated in rare neurodevelopmental disorders, highlighting its importance in neuronal function.
Recombinant THG1L protein is engineered for in vitro studies to dissect its molecular mechanisms. Produced via bacterial or mammalian expression systems, it enables investigations into protein-protein interactions, enzymatic activity, and drug screening. Researchers utilize it to explore therapeutic strategies targeting mitochondrial dysfunction or cancer metabolism. Despite progress, THG1L’s full interactome and disease-specific roles remain under investigation, underscoring its potential as a biomarker or therapeutic target in precision medicine.
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