| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TR |
| Uniprot No | Q8IYR6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 40-330aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSSNQPPGGGGGSGGDCPGGKGKSINCSE LNVRESDVRVCDESSCKYGGVCKEDGDGLKCACQFQCHTNYIPVCGSNGD TYQNECFLRRAACKHQKEITVIARGPCYSDNGSGSGEGEEEGSGAEVHRK HSKCGPCKYKAECDEDAENVGCVCNIDCSGYSFNPVCASDGSSYNNPCFV REASCIKQEQIDIRHLGHCTDTDDTSLLGKKDDGLQYRPDVKDASDQRED VYIGNHMPCPENLNGYCIHGKCEFIYSTQKASCRCESGYTGQHCEKTDFS ILYVVPSRQKLTHV |
| 预测分子量 | 34 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. |
以下是关于甲状腺激素受体(Thyroid Hormone Receptor, TR)重组蛋白研究的3篇代表性文献，内容为模拟概括：
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1. **文献名称**: *"Expression and Purification of Functional Thyroid Hormone Receptor Isoforms from Escherichia coli"*
**作者**: Smith J, et al.
**摘要**: 研究报道了在大肠杆菌中高效表达并纯化具有生物活性的TRα和TRβ重组蛋白，通过优化表达条件和亲和层析技术获得高纯度蛋白，验证其与DNA结合及配体(T3)结合能力，为后续结构功能研究奠定基础。
2. **文献名称**: *"Crystal Structure of the Thyroid Hormone Receptor Ligand-Binding Domain Reveals a Flexible Mechanism of Hormone Recognition"*
**作者**: Rodriguez A, et al.
**摘要**: 通过X射线晶体学解析TRβ配体结合域与甲状腺激素T3的复合物结构，揭示受体通过构象变化适配配体结合的分子机制，阐明了突变导致激素抵抗症的分子基础。
3. **文献名称**: *"High-Throughput Screening of Small Molecule Modulators of Thyroid Hormone Receptor Using a Luciferase Reporter Assay"*
**作者**: Chen L, et al.
**摘要**: 开发基于TR重组蛋白和荧光素酶报告基因的高通量筛选平台，成功筛选出新型TR激动剂和拮抗剂，为甲状腺功能异常及相关癌症的药物开发提供先导化合物。
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**说明**：
- 上述文献为示例，实际文献需通过PubMed/Google Scholar检索关键词“recombinant thyroid hormone receptor”或“TR protein purification/mechanism/screening”获取。
- 若“TR”指其他蛋白(如Toll-like Receptor、Testosterone Receptor等)，建议补充具体背景以便精准推荐。
**Background of TR Recombinant Proteins**
TR (Thioredoxin Reductase) recombinant proteins are engineered variants of the naturally occurring thioredoxin reductase enzyme, a critical component of the thioredoxin system responsible for maintaining cellular redox homeostasis. This system plays a vital role in regulating oxidative stress, DNA synthesis, and apoptosis. TR enzymes, typically NADPH-dependent flavoproteins, catalyze the reduction of thioredoxin (Trx), which in turn reduces disulfide bonds in target proteins, supporting antioxidant defense and redox signaling.
Recombinant TR proteins are produced using genetic engineering techniques, where the TR gene is cloned into expression vectors and expressed in host systems like *E. coli*, yeast, or mammalian cells. These systems enable large-scale production of TR with high purity and activity, often incorporating affinity tags (e.g., His-tag) for simplified purification. Recombinant TR proteins retain the functional properties of native enzymes, including substrate specificity and catalytic efficiency, making them valuable tools for biochemical and biomedical research.
Applications of TR recombinant proteins span drug discovery, enzymology, and disease mechanism studies. They are used to screen inhibitors targeting TR activity, as dysregulated TR is implicated in cancer, neurodegenerative diseases, and parasitic infections. Additionally, TR fusion proteins are employed in structural studies to resolve enzyme mechanisms and design therapeutics. Challenges in their production include maintaining proper folding and post-translational modifications in prokaryotic hosts, which may require optimization of expression conditions or use of eukaryotic systems.
Recent advances in protein engineering, such as codon optimization and CRISPR-based editing, have enhanced TR recombinant protein yield and functionality. Their versatility continues to drive innovations in redox biology, highlighting their importance in both basic research and therapeutic development.
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