| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | disA |
| Uniprot No | Q743W9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-357aa |
| 氨基酸序列 | MTRPTLRETVARLAPGTGLRDGLERILRGRTGALIVLGNDENVEAICDGGFALDVRYAPTRLRELAKMDGAVVLSTDGSRIVRANVQLVPDPSIATDESGTRHRSAERAAIQTGYPVISVSHSMNIVTVYVGGERHVVADSATILSRANQAIATLERYKIRLDEVSRQLSRAEIEDFVTLRDVLTVVQRLELVRRIGQVIDNDVVELGTDGRQLRLQLDELLGGNDNARELIVRDYHASPEQLSEAQMTATLDELDALSDTELLDFTALAKVFGYPTTTEAQDSAVSPRGYRALAGIPRLQFAHADLLVRSFGTLQNVLAASASDLQSIDGIGAMWARHVREGLSQLAESTITDSLS |
| 预测分子量 | 45.9 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DisA重组蛋白的3篇代表性文献示例(注：内容为模拟示例，非真实文献)：
1. **文献名称**：*DisA monitors DNA replication and sporulation in Bacillus subtilis*
**作者**：Bejerano-Sagie, M., et al.
**摘要**：该研究揭示了枯草芽孢杆菌中DisA蛋白通过合成第二信使c-di-AMP，实时监测DNA复制完整性，并在DNA损伤时延迟孢子形成，协调细胞周期与应激响应。
2. **文献名称**：*Structural basis for c-di-AMP synthesis by the DNA integrity scanner DisA*
**作者**：Witte, G., et al.
**摘要**：通过晶体学分析，阐明DisA蛋白的寡聚化结构及催化中心机制，证明其双酶活性(c-di-AMP合成酶与DNA结合能力)在DNA损伤修复中的协同作用。
3. **文献名称**：*DisA-like proteins in mycobacteria link DNA repair to virulence*
**作者**：Kiran, M., et al.
**摘要**：发现结核分枝杆菌中DisA同源蛋白通过调控c-di-AMP水平影响毒力基因表达，提示DisA家族在病原菌应激生存与宿主感染中的潜在作用。
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**注**：以上为基于领域知识的模拟文献，实际引用请通过PubMed/Google Scholar以“DisA protein recombination”、“DisA c-di-AMP”等关键词检索近期论文。
**Background of disA Recombinant Protein**
DisA (DNA integrity scanning protein A) is a conserved bacterial protein initially characterized in *Bacillus subtilis*. It plays a dual role in monitoring chromosomal DNA integrity and regulating sporulation, a survival mechanism under stress. Structurally, disA forms an octameric complex with a unique dumbbell-shaped architecture, featuring a central catalytic domain with diadenylate cyclase activity. This domain synthesizes the secondary messenger cyclic di-AMP (c-di-AMP), a signaling molecule critical for bacterial stress adaptation, cell wall homeostasis, and biofilm formation.
DisA acts as a checkpoint protein during sporulation. It scans the chromosome for DNA damage, and if lesions are detected, it halts sporulation by reducing c-di-AMP production, thereby allowing time for repair. This mechanism ensures genomic stability before cells commit to forming stress-resistant spores. The protein’s ability to bind branched DNA structures (e.g., Holliday junctions) further underscores its role in DNA repair and recombination processes.
Recombinant disA protein is produced via heterologous expression systems, such as *E. coli*, enabling detailed biochemical and structural studies. Its recombinant form has been pivotal in elucidating c-di-AMP signaling pathways and dissecting disA’s enzymatic and DNA-binding activities. Researchers also explore disA’s potential applications in synthetic biology, antimicrobial drug development (by targeting c-di-AMP pathways), and as a tool to study bacterial stress responses.
Overall, disA exemplifies a critical nexus between bacterial DNA repair, signaling, and developmental regulation, making it a focal point in both basic microbiology and applied biotechnology research.
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