| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ykuP |
| Uniprot No | O34589 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-151aa |
| 氨基酸序列 | MAKILLVYATMSGNTEAMADLIEKGLQEALAEVDRFEAMDIDDAQLFTDYDHVIMGTYTWGDGDLPDEFLDLVEDMEEIDFSGKTCAVFGSGDTAYEFFCGAVDTLEAKIKERGGDIVLPSVKIENNPEGEEEEELINFGRQFAKKSGCAV |
| 预测分子量 | 32.6 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ykuP重组蛋白的参考文献示例(注：内容为模拟虚构，实际文献需通过学术数据库验证)：
1. **文献名称**：*Functional Characterization of ykuP in Bacillus subtilis Cell Wall Stress Response*
**作者**：Hashimoto M., et al. (2009)
**摘要**：研究通过克隆并表达ykuP重组蛋白，发现其在枯草芽孢杆菌中参与细胞壁损伤修复，体外实验表明ykuP具有肽聚糖水解酶活性，可能与细胞壁重塑相关。
2. **文献名称**：*Structural Insights into ykuP: A Putative Lytic Transglycosylase in Gram-Positive Bacteria*
**作者**：Svensson K., Claessen D. (2012)
**摘要**：解析了ykuP重组蛋白的晶体结构，揭示其与真核Ku蛋白的结构差异，提出其可能通过溶菌酶活性参与细菌细胞壁代谢，为抗菌靶点开发提供依据。
3. **文献名称**：*ykuP Interaction with DNA Repair Complexes in Staphylococcus aureus*
**作者**：Smith R., et al. (2015)
**摘要**：利用重组ykuP蛋白进行Pull-down实验，证明其与S. aureus中RecA蛋白互作，提示其在DNA损伤修复中的潜在辅助功能，尤其在氧化应激条件下表达上调。
4. **文献名称**：*Recombinant ykuP Expression Optimization and Antibiotic Susceptibility Analysis*
**作者**：Tanaka Y., et al. (2018)
**摘要**：优化了ykuP在大肠杆菌中的可溶性表达条件，并通过体外抑制实验发现ykuP缺失株对β-内酰胺类抗生素敏感性增强，表明其可能参与耐药性调控。
**建议**：以上为模拟示例，实际文献请通过PubMed或Google Scholar搜索关键词“ykuP recombinant protein”或“ykuP function”获取最新研究。
The ykuP recombinant protein is derived from the ykuP gene, originally identified in *Bacillus subtilis* and related Gram-positive bacteria. This gene encodes a protein homologous to the Ku family, which is evolutionarily conserved across prokaryotes and eukaryotes. In bacterial systems, YkuP forms a heterodimer with YkuD, functioning as a critical component in the non-homologous end joining (NHEJ) DNA repair pathway. Unlike homologous recombination, NHEJ enables direct ligation of double-strand DNA breaks (DSBs) without requiring a repair template, making it vital for survival under conditions of oxidative stress or desiccation. YkuP’s role in stabilizing broken DNA ends and recruiting ligases highlights its importance in maintaining genomic integrity, particularly in stationary-phase cells where replication is limited.
Structurally, YkuP contains conserved domains for ATP binding and DNA end recognition, facilitating its interaction with broken DNA termini. Studies using X-ray crystallography have revealed its dimeric architecture, which clamps around DNA to protect against nucleolytic degradation. Recombinant YkuP is typically produced in *E. coli* expression systems, purified via affinity chromatography, and utilized in *in vitro* assays to dissect NHEJ mechanisms. Its simplicity compared to eukaryotic Ku proteins (which require DNA-PKcs for activity) makes it a model for studying DSB repair fundamentals.
Research on YkuP has broader implications for understanding genome stability in pathogens, optimizing CRISPR-Cas9 gene-editing tools (by improving DSB repair efficiency), and developing antimicrobial strategies targeting bacterial stress response pathways. Recent work also explores engineered variants of YkuP to enhance synthetic biology applications, such as stabilizing synthetic DNA constructs. Despite its prokaryotic origin, insights from YkuP continue to inform eukaryotic DNA repair studies, bridging evolutionary gaps in genome maintenance mechanisms.
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