| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Z |
| Uniprot No | Q8WXG8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-99aa |
| 氨基酸序列 | MPTQLEMAMDTMIRIFHRYSGKERKRFKLSKGELKLLLQRELTEFLSCQKETQLVDKIVQDLDANKDNEVDFNEFVVMVAALTVACNDYFVEQLKKKGK |
| 预测分子量 | 11,6 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“Z重组蛋白”的3篇示例文献(注：内容基于学术文献常见结构模拟，非真实文献)：
---
1. **《高效表达重组Z蛋白的大肠杆菌系统优化研究》**
**作者**：Smith, J. et al.
**摘要**：本研究通过密码子优化和诱导条件筛选，在大肠杆菌中实现重组Z蛋白的高效可溶性表达，纯化后蛋白具备预期的生物活性，为大规模生产奠定基础。
2. **《重组Z蛋白调控细胞凋亡的分子机制》**
**作者**：Wang, Y. et al.
**摘要**：通过体外实验证实，重组Z蛋白能特异性结合凋亡相关信号分子，抑制肿瘤细胞增殖，揭示了其在癌症治疗中的潜在应用价值。
3. **《基于哺乳动物细胞的重组Z蛋白糖基化修饰分析》**
**作者**：Zhang, L. et al.
**摘要**：利用CHO细胞系统表达重组Z蛋白，结合质谱技术解析其糖基化修饰模式，证明糖链结构对蛋白稳定性和功能具有关键影响。
---
**说明**：若需真实文献，建议在PubMed或Google Scholar中搜索关键词(如“recombinant Z protein”或“Z-protein expression”)，并结合具体研究领域筛选。
**Background of Z-Recombinant Proteins**
Z-recombinant proteins, often referred to in the context of Z-DNA/RNA-binding proteins, are a class of molecules that interact with left-handed Z-form nucleic acids, a structural variant distinct from the canonical right-handed B-DNA. Discovered in the 1970s, Z-DNA forms under physiological conditions such as high salt concentrations, negative supercoiling, or specific base modifications. Proteins binding to Z-DNA/Z-RNA, like the Zα domain-containing proteins (e.g., ADAR1. ZBP1. and PKZ), play critical roles in immune response regulation, gene expression, and viral defense mechanisms.
The Zα domain, a conserved structural motif, enables specific recognition of Z-form nucleic acids. For instance, ADAR1. an RNA-editing enzyme, utilizes its Zα domain to bind Z-RNA, influencing innate immune signaling by preventing aberrant activation of cytosolic nucleic acid sensors. Similarly, ZBP1 (Z-DNA-binding protein 1) triggers necroptosis upon detecting Z-RNA during viral infections or cellular stress, highlighting its role in antiviral defense and inflammation.
Research on Z-recombinant proteins has expanded due to their implications in diseases. Dysregulation of Z-DNA/RNA-protein interactions is linked to autoimmune disorders (e.g., Aicardi-Goutières syndrome) and cancers. Additionally, pathogens like vaccinia virus encode Zα proteins to evade host immunity, underscoring their evolutionary significance.
Biotechnological applications of Z-recombinant proteins include engineered enzymes for nucleic acid sensing and gene-editing tools. Their unique binding specificity also inspires drug development targeting Z-form nucleic acid-protein interactions in oncology and virology. Continued studies aim to unravel their structural dynamics and therapeutic potential, bridging molecular biology and clinical innovation.
×
