| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TBP |
| Uniprot No | P20226 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-339aa |
| 氨基酸序列 | MDQNNSLPPYAQGLASPQGAMTPGIPIFSPMMPYGTGLTPQPIQNTNSLSILEEQQRQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQAVAAAAVQQSTSQQATQGTSGQAPQLFHSQTLTTAPLPGTTPLYPSPMTPMTPITPATPASESSGIVPQLQNIVSTVNLGCKLDLKTIALRARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEEQSRLAARKYARVVQKLGFPAKFLDFKIQNMVGSCDVKFPIRLEGLVLTHQQFSSYEPELFPGLIYRMIKPRIVLLIFVSGKVVLTGAKVRAEIYEAFENIYPILKGFRKTT |
| 预测分子量 | 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TBP(TATA结合蛋白)重组蛋白研究的参考文献及摘要概括：
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1. **文献名称**：*Crystal structure of a TBP/TATA-box complex*
**作者**：Nikolov DB, Hu SH, Lin J, Gasch A, Hoffmann A, Horikoshi M, Chua NH, Roeder RG, Burley SK
**摘要**：该研究通过X射线晶体学解析了人源TBP重组蛋白与TATA-box DNA复合体的三维结构，揭示了TBP如何通过β折叠与DNA小沟结合，为理解真核转录起始机制提供了结构基础。
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2. **文献名称**：*Recombinant TBP from Saccharomyces cerevisiae: cloning, expression, and purification*
**作者**：Hernandez HM, Schmidt MC
**摘要**：报道了利用大肠杆菌表达系统高效表达和纯化酵母来源重组TBP的方法，验证其与TATA-box DNA的结合活性，为体外转录研究提供了标准化蛋白制备方案。
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3. **文献名称**：*Functional analysis of TBP mutations in transcriptional activation*
**作者**：Lieberman PM, Schmidt MC
**摘要**：通过构建重组TBP突变体，系统研究其与TFIID复合体及RNA聚合酶II的相互作用，发现N端结构域对转录激活的关键调控作用，揭示TBP在基因选择性表达中的分子机制。
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以上文献均聚焦于TBP重组蛋白的结构、制备及功能研究，涵盖基础机制与实验技术。
**Background of TBP Recombinant Protein**
The TATA-binding protein (TBP) is a critical transcription factor involved in the initiation of RNA polymerase II-mediated transcription across eukaryotes. It serves as a core component of the TFIID complex, which binds to the TATA-box DNA sequence in gene promoters, facilitating the assembly of the pre-initiation complex (PIC) and recruiting other general transcription factors. TBP’s highly conserved C-terminal domain adopts a saddle-like structure that directly interacts with the minor groove of the TATA-box, inducing DNA bending and stabilizing promoter recognition.
Recombinant TBP proteins are engineered using genetic cloning techniques, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., yeast, insect cells) to ensure proper folding and post-translational modifications. These proteins retain the functional domains required for DNA binding and interactions with transcription regulators, making them indispensable tools for *in vitro* studies of transcriptional mechanisms. Researchers employ TBP recombinant proteins to dissect its role in nucleating PIC assembly, modulating promoter specificity, and coordinating with coactivators or repressors.
Additionally, TBP variants linked to neurodegenerative diseases (e.g., spinocerebellar ataxias) or transcriptional dysregulation are often studied using recombinant forms to analyze mutation effects on DNA binding, protein stability, or interaction networks. Structural studies (e.g., X-ray crystallography, cryo-EM) leveraging recombinant TBP have also elucidated conformational changes during transcription initiation. Overall, TBP recombinant proteins are pivotal in advancing our understanding of gene regulation and developing therapeutic strategies targeting transcriptional machinery.
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