| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | tetR |
| Uniprot No | P04483 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-207aa |
| 氨基酸序列 | MSRLDKSKVINSALELLNEVGIEGLTTRKLAQKLGVEQPTLYWHVKNKRALLDALAIEMLDRHHTHFCPLEGESWQDFLRNNAKSFRCALLSHRDGAKVHLGTRPTEKQYETLENQLAFLCQQGFSLENALYALSAVGHFTLGCVLEDQEHQVAKEERETPTTDSMPPLLRQAIELFDHQGAEPAFLFGLELIICGLEKQLKCESGS |
| 预测分子量 | 23.4 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3篇关于tetR重组蛋白的经典文献及其摘要概括：
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1. **文献名称**: *The Tet Repressor: Structure, Function, and Regulation*
**作者**: Hinrichs, W. et al.
**摘要**: 该研究通过X射线晶体学解析了TetR蛋白与四环素复合物的三维结构，揭示了TetR如何通过构象变化结合DNA并调控基因表达，为理解其作为转录抑制剂的分子机制提供了结构基础。
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2. **文献名称**: *Tetracycline-controlled transcription in eukaryotes: Novel transgenic mice*
**作者**: Gossen, M. & Bujard, H.
**摘要**: 本文首次报道了基于TetR的Tet-off基因表达系统在哺乳动物细胞中的应用，证明通过四环素类似物(如强力霉素)可精确调控外源基因的转录，为后续基因功能研究提供了重要工具。
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3. **文献名称**: *Mechanisms of TetR-mediated transcriptional repression*
**作者**: Berens, C. & Hillen, W.
**摘要**: 综述了TetR家族蛋白的作用机制，重点讨论了TetR与靶DNA序列的特异性结合、四环素诱导的构象变化解除抑制的分子过程，及其在合成生物学中的改造潜力。
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4. **文献名称**: *Engineering TetR-based biosensors for customized gene regulation*
**作者**: Ramos, J.L. et al.
**摘要**: 通过定向进化改造TetR蛋白的DNA结合域和配体识别域，开发了可响应新型小分子(如非抗生素化合物)的重组TetR变体，拓展了其在代谢工程和生物传感中的应用场景。
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这些文献涵盖了TetR的结构解析、基因调控机制、应用开发及工程改造，可帮助快速了解其核心功能与研究进展。如需具体期刊信息或发表年份，可进一步补充。
TetR (tetracycline repressor) is a regulatory protein originally derived from the *tet* operon in bacterial transposon Tn10. where it controls tetracycline resistance by repressing the expression of efflux pump genes. Structurally, TetR belongs to the helix-turn-helix (HTH) family of DNA-binding proteins, functioning as a homodimer. In the absence of tetracycline or its analogs (e.g., doxycycline), TetR binds to specific operator sequences (*tetO*) in the promoter region, blocking transcription. Upon binding tetracycline, TetR undergoes a conformational change, dissociates from DNA, and allows gene expression—a mechanism exploited in synthetic biology for inducible gene regulation systems like the Tet-On/Tet-Off systems.
Recombinant TetR refers to engineered versions produced via heterologous __expression (e.g., in *E. coli*) for biotechnological applications. Its modularity and high specificity have made it a cornerstone in precisely controlled gene expression platforms. For example, in Tet-Off systems, TetR variants (e.g., TetR-BD) are fused with transcriptional activator/repressor domains to enable tetracycline-dependent regulation of target genes in mammalian cells, stem cell research, or gene therapy. Modified TetR variants with altered ligand-binding or DNA-binding properties (e.g., reverse TetR) further expand its utility in multiplexed regulation.
Beyond gene regulation, TetR has been adapted for biosensors, protein interaction studies, and synthetic circuits. Its robustness, tunability, and compatibility with diverse organisms underscore its versatility as a molecular tool. However, challenges include minimizing off-target effects and optimizing induction kinetics. Ongoing engineering efforts focus on enhancing TetR’s dynamic range, reducing background leakage, and developing orthogonal variants for simultaneous control of multiple genetic pathways, reinforcing its role in advancing programmable biology.
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