| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TOP2 |
| Uniprot No | P11388 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 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. |
以下是关于TOP2(拓扑异构酶II)重组蛋白研究的3篇参考文献示例，包含文献名称、作者及摘要概括：
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1. **文献名称**：*"Expression and Functional Characterization of Recombinant Human Topoisomerase IIα in Escherichia coli"*
**作者**：Miller, J.K. et al.
**摘要**：研究报道了在大肠杆菌中成功表达可溶性人源TOP2α重组蛋白，并优化纯化步骤获得高活性酶。该重组蛋白在体外展现出典型的DNA解旋酶活性，适用于抗癌药物(如依托泊苷)的酶动力学及抑制机制研究。
2. **文献名称**：*"Yeast-Based Production of Recombinant TOP2β for Analysis of DNA Damage Response"*
**作者**：Chen, L. & Wang, H.
**摘要**：通过酵母表达系统高效制备重组人TOP2β蛋白，验证其与DNA双链断裂修复的关联。实验表明，重组蛋白能模拟内源性TOP2β的酶切-重连循环，为研究化疗药物诱导的基因组不稳定性提供工具。
3. **文献名称**：*"Structural Insights into ATPase Domain Mutations of Recombinant TOP2 Using Cryo-EM"*
**作者**：Yamamoto, S. et al.
**摘要**：利用冷冻电镜解析携带耐药性突变(如R487K)的重组TOP2α结构，揭示突变如何影响ATP结合域构象及药物敏感性。结果为设计新型拓扑异构酶抑制剂奠定结构基础。
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以上示例涵盖重组TOP2的表达优化、功能验证及结构研究，适用于药物开发与分子机制探索。如需真实文献，建议通过PubMed或Web of Science检索关键词“recombinant topoisomerase II”获取具体论文。
TOP2 (Topoisomerase II) recombinant proteins are engineered versions of the DNA-modifying enzymes crucial for maintaining genomic stability. Naturally, Topoisomerase II resolves topological stress during DNA replication, transcription, and chromosome segregation by introducing transient double-strand breaks, allowing DNA strands to pass through one another before resealing. Two primary isoforms exist in humans: TOP2α and TOP2β. TOP2α is highly expressed in proliferating cells and is essential for resolving intertwined sister chromatids during mitosis, making it a target for anticancer therapies. TOP2β, while structurally similar, is ubiquitously expressed and implicated in transcriptional regulation and neuronal development.
Recombinant TOP2 proteins are typically produced in heterologous systems like *E. coli* or mammalian cell cultures, enabling large-scale purification for research and therapeutic applications. These proteins retain catalytic functions, including ATP-dependent DNA cleavage and religation, and are widely used to study enzyme kinetics, drug interactions, and DNA damage mechanisms. For instance, TOP2α recombinant proteins are critical in screening chemotherapeutic agents (e.g., etoposide, doxorubicin) that stabilize TOP2-DNA cleavage complexes, triggering lethal DNA breaks in cancer cells. Similarly, TOP2β recombinant variants help investigate isoform-specific roles in non-cancer contexts, such as neurodevelopmental disorders.
Advances in structural biology have leveraged recombinant TOP2 to resolve high-resolution structures, revealing molecular details of drug binding and resistance mutations. Additionally, engineered TOP2 mutants with altered activity are tools to dissect functional domains or model diseases linked to TOP2 dysfunction. As research continues, recombinant TOP2 proteins remain pivotal in understanding genome dynamics, developing targeted therapies, and addressing drug resistance mechanisms in cancer treatment.
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