| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | yafQ |
| Uniprot No | Q47149 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-92aa |
| 氨基酸序列 | MIQRDIEYSG QYSKDVKLAQ KRHKDMNKLK YLMTLLINNT LPLPAVYKDH PLQGSWKGYR DAHVEPDWIL IYKLTDKLLR FERTGTHAAL FG |
| 预测分子量 | 10,8 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yafQ重组蛋白的3篇文献示例(仅供参考，建议通过学术数据库核实)：
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1. **文献名称**：*Crystal structure of the YafQ protein from Escherichia coli reveals a tandem dimer resembling an ubiquitin ligase*
**作者**：Christensen-Dalsgaard M, Gerdes K
**摘要**：解析了YafQ重组蛋白的晶体结构，发现其以串联二聚体形式存在，结构类似泛素连接酶，暗示其可能参与蛋白质降解调控，与DinJ抗毒素结合后形成异源四聚体复合物。
2. **文献名称**：*YafQ is an mRNA interferase regulated by the antitoxin DinJ*
**作者**：Zhang Y, Zhang J, et al.
**摘要**：研究表明重组YafQ蛋白具有核糖核酸酶活性，通过切割特定mRNA抑制细菌翻译，其毒性活性依赖DinJ抗毒素的动态调控，揭示了毒素-抗毒素系统在细菌胁迫适应中的作用。
3. **文献名称**：*Recombinant YafQ expression and its role in bacterial persister formation*
**作者**：Kamruzzaman M, Ito C
**摘要**：通过重组YafQ蛋白的体外表达与功能分析，发现其可诱导大肠杆菌进入休眠状态(持留菌表型)，并证实其核酶活性是触发细菌应激反应的关键因素。
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**注意**：以上文献为模拟示例，实际文献需通过PubMed、Google Scholar等平台检索关键词(如“YafQ recombinant protein”“YafQ-DinJ complex”)获取。
**Background of YafQ Recombinant Protein**
YafQ is a bacterial toxin protein belonging to the YafQ-DinJ toxin-antitoxin (TA) system, predominantly studied in *Escherichia coli*. TA systems are genetic modules widely conserved in bacteria and archaea, typically comprising a toxin that inhibits essential cellular processes (e.g., translation, DNA replication) and an antitoxin that neutralizes the toxin’s activity. These systems are implicated in stress adaptation, biofilm formation, and persister cell formation, aiding bacterial survival under adverse conditions.
The YafQ toxin functions by cleaving mRNA in a ribosome-dependent manner, stalling translation and inducing growth arrest. Its activity is counteracted by DinJ, a labile antitoxin that forms a stable complex with YafQ under normal conditions. Under stress (e.g., nutrient deprivation), proteases degrade DinJ, releasing YafQ to exert its toxic effects. This dynamic regulation helps bacteria enter a dormant state, promoting survival until conditions improve.
Recombinant YafQ protein, produced via heterologous expression in *E. coli* or other expression systems, has been pivotal in elucidating its structural and functional mechanisms. Structural studies reveal that YafQ adopts a ferredoxin-like fold and binds to the ribosomal exit tunnel, mimicking elongation factors. Its ribosome-dependent mRNA cleavage activity distinguishes it from other RNase toxins like RelE.
Research on YafQ recombinant protein has broader implications. It serves as a model to study TA system regulation and bacterial persistence, a key factor in antibiotic tolerance. Additionally, engineered TA systems, including YafQ-DinJ, are explored as tools for plasmid maintenance in biotechnology or as targets for novel antimicrobial strategies. Understanding YafQ’s role may inform approaches to disrupt bacterial stress responses, potentially overcoming treatment-resistant infections.
Overall, YafQ recombinant protein studies bridge fundamental microbiology and applied biomedical research, highlighting its significance in both bacterial physiology and therapeutic innovation.
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