| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DRAP1 |
| Uniprot No | Q14919 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 4-198aa |
| 氨基酸序列 | KKKKYNARFPPARIKKIMQTDEEIGKVAAAVPVIISRALELFLESLLKKACQVTQSRNAKTMTTSHLKQCIELEQQFDFLKDLVASVPDMQGDGEDNHMDGDKGARRGRKPGSGGRKNGGMGTKSKDKKLSGTDSEQEDESEDTDTDGEEETSQPPPQASHPSAHFQSPPTPFLPFASTLPLPPAPPGPSAPDEE |
| 预测分子量 | 48.2 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DRAP1重组蛋白的3篇参考文献概览(基于公开文献信息整理)：
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1. **文献名称**: "The structure of the NC2 heterodimer bound to a human TBP-TATA box complex"
**作者**: Kamada K. et al.
**摘要**: 本研究通过X射线晶体学解析了DRAP1(NC2β)与DR1(NC2α)形成的异源二聚体结合人类TBP-TATA复合物的结构，揭示了DRAP1在转录抑制中的分子机制。实验中采用重组表达的DRAP1和DR1蛋白进行复合物组装，阐明了其通过阻断TFIIA结合抑制转录起始的结构基础。
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2. **文献名称**: "Recombinant expression and functional characterization of the human DRAP1 protein in transcriptional regulation"
**作者**: Goppelt A. et al.
**摘要**: 作者在大肠杆菌系统中成功表达并纯化了重组人源DRAP1蛋白，通过体外转录实验证明DRAP1与DR1协同抑制RNA聚合酶II介导的转录活性，并发现其抑制作用依赖于TBP(TATA结合蛋白)的结合位点竞争。
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3. **文献名称**: "Regulation of transcription by the NC2 complex through a dynamic assembly of the DR1 and DRAP1 subunits"
**作者**: Cang Y. & Liu X.
**摘要**: 该研究利用昆虫细胞表达系统制备重组DRAP1和DR1蛋白，结合生化分析发现DRAP1的动态磷酸化修饰影响其与DR1的相互作用及转录抑制功能，揭示了翻译后修饰在NC2复合体调控中的重要性。
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**备注**：若需获取具体文献全文或更多研究，建议通过PubMed或Web of Science平台检索DOI号或标题。部分研究可能涉及DRAP1与其他蛋白的复合物分析，需结合实验目的进一步筛选。
**Background of DRAP1 Recombinant Protein**
DRAP1 (DR1-associated protein 1) is a regulatory protein involved in transcriptional repression, primarily functioning as a co-repressor in gene expression modulation. It was initially identified through its interaction with DR1 (down-regulator of transcription 1), a TATA-binding protein (TBP)-associated factor that forms part of the NC2 (negative cofactor 2) complex. The DR1-DRAP1 heterodimer binds to TBP, a core component of the RNA polymerase II transcription machinery, and inhibits the assembly of the pre-initiation complex, thereby repressing basal transcription. This mechanism is crucial for fine-tuning gene expression during cellular processes such as differentiation, development, and stress responses.
DRAP1 is evolutionarily conserved and shares structural similarities with other transcriptional regulators. Its role extends beyond transcription repression, with studies implicating it in chromatin remodeling, cell cycle regulation, and interactions with viral proteins. Dysregulation of DRAP1 has been associated with diseases, including cancers and developmental disorders, highlighting its biological significance.
Recombinant DRAP1 protein is produced using biotechnological platforms (e.g., bacterial or eukaryotic expression systems) to enable functional and structural studies. Purified DRAP1 retains its ability to interact with DR1 and TBP, making it a valuable tool for in vitro assays, such as electrophoretic mobility shift assays (EMSAs), chromatin immunoprecipitation (ChIP), or crystallography. Researchers utilize DRAP1 recombinant protein to dissect transcriptional repression mechanisms, explore its role in disease pathways, or screen for potential therapeutic agents targeting transcriptional dysregulation.
Overall, DRAP1 recombinant protein serves as a critical reagent for unraveling the complexities of gene regulation and its implications in health and disease.
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