| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | tpd |
| Uniprot No | P19478 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-204aa |
| 氨基酸序列 | CGGGGEHQHGEEMMAAVPAPDAEGAAGFDEFPIGEDRDVGPLHVGGVYFQPVEMHPAPGAQPSKEEADCHIEADIHANEAGKDLGYGVGDFVPYLRVVAFLQKHGSEKVQKVMFAPMNAGDGPHYGANVKFEEGLGTYKVRFEIAAPSHDEYSLHIDEQTGVSGRFWSEPLVAEWDDFEWKGPQW |
| 预测分子量 | 27.1 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. |
以下是关于靶向蛋白降解(Targeted Protein Degradation, TPD)领域中重组蛋白应用的模拟参考文献示例，供参考：
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1. **《Design and Application of Bifunctional PROTACs Using Recombinant E3 Ligases》**
*作者：Crews, K.D., Sakamoto, T.*
**摘要**：本研究利用重组表达的E3连接酶(如VHL和CRBN)设计新型PROTAC分子，通过体外重组蛋白筛选验证了其降解靶蛋白的效力，为癌症治疗提供了新策略。
2. **《Recombinant Protein Engineering for Enhanced Targeted Degradation Efficiency》**
*作者：Békés, M., Winter, G.E.*
**摘要**：通过重组蛋白技术优化分子胶降解剂的结合界面，解析了降解复合物的晶体结构，揭示了重组蛋白在TPD分子设计中的关键作用。
3. **《Development of a High-Throughput Screening Platform for TPD Using Recombinant Proteins》**
*作者：Mullard, A., Lu, J.*
**摘要**：构建基于重组靶蛋白和E3连接酶的体外高通量筛选体系，成功筛选出小分子降解剂，加速了TPD药物的早期开发流程。
4. **《Challenges in Recombinant Protein Production for Degrader-Based Therapies》**
*作者：Zhou, P., Craig, R.W.*
**摘要**：探讨重组蛋白表达纯化在TPD应用中的技术难点，提出通过定向进化改善E3连接酶稳定性的方法，以提升降解剂功能。
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**说明**：以上为模拟参考文献，实际文献需通过PubMed、Web of Science等平台检索确认。建议使用关键词“Targeted Protein Degradation recombinant protein”或结合具体蛋白名称进行精准查询。
**Background of TPD-Based Recombinant Proteins**
Targeted protein degradation (TPD) has emerged as a transformative strategy in drug discovery, leveraging cellular machinery to eliminate disease-causing proteins. Traditional small-molecule inhibitors often require continuous target engagement and struggle with "undruggable" targets, such as non-enzymatic proteins or those lacking defined binding pockets. TPD overcomes these limitations by using bifunctional molecules to recruit E3 ubiquitin ligases, marking specific proteins for proteasomal degradation.
Recombinant proteins play a pivotal role in advancing TPD technologies. For instance, proteolysis-targeting chimeras (PROTACs), a leading TPD approach, rely on recombinant proteins for structural optimization and functional validation. These chimeric molecules combine a target-binding domain (often derived from recombinant antibodies or ligands) with a ligase-recruiting moiety, enabling selective degradation. Recombinant expression systems (e.g., *E. coli*, mammalian cells) are critical for producing functional components of PROTACs, including engineered ubiquitin ligases or target-binding domains with enhanced specificity.
Recent innovations, such as molecular glues and heterobifunctional degraders, further highlight the synergy between recombinant protein engineering and TPD. For example, recombinant crystallographic studies have elucidated degradation mechanisms, while phage display libraries expedite ligand discovery for novel targets. Clinical progress, including PROTACs like ARV-110 (targeting AR in prostate cancer) and ARV-471 (targeting ER in breast cancer), underscores the therapeutic potential.
Challenges remain, such as optimizing pharmacokinetics and minimizing off-target effects. However, the integration of recombinant protein technologies with TPD continues to expand the druggable proteome, offering hope for cancers, neurodegenerative disorders, and infectious diseases. As of 2023. over 20 TPD-based therapies are in clinical trials, marking a paradigm shift in precision medicine.
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