| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | relG |
| Uniprot No | O33348 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-87aa |
| 氨基酸序列 | MPYTVRFTTTARRDLHKLPPRILAAVVEFAFGDLSREPLRVGKPLRRELAGTFSARRGTYRLLYRIDDEHTTVVILRVDHRADIYRR |
| 预测分子量 | 26.2 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RelG重组蛋白的模拟参考文献示例，供参考：
1. **标题**：Heterologous Expression and Purification of RelG Recombinant Protein in *Escherichia coli*
**作者**：Smith, J.R.; Tanaka, K.; Müller, A.
**期刊**：*Protein Expression and Purification*, 2018. Vol. 150. pp. 45-52.
**摘要**：本研究成功构建了RelG重组蛋白的原核表达系统，通过优化诱导条件在大肠杆菌中实现高效可溶性表达，并利用镍柱亲和层析获得高纯度蛋白，为后续酶学分析奠定基础。
2. **标题**：Enzymatic Characterization of RelG: A Novel (p)ppGpp Synthase in Bacterial Stress Response
**作者**：Chen, L.; Wang, H.; González-Bello, C.
**期刊**：*Journal of Biological Chemistry*, 2020. Vol. 295. No. 12. pp. 3987-3999.
**摘要**：通过体外酶活实验证实RelG具有依赖核糖体的(p)ppGpp合成酶活性，其催化效率受氨基酸饥饿信号调控，揭示了RelG在细菌严谨反应中的潜在作用机制。
3. **标题**：Crystal Structure of RelG Recombinant Protein Reveals Unique Substrate-Binding Motifs
**作者**：Yamamoto, S.; Ohta, N.; Zhang, R.
**期刊**：*Nature Structural & Molecular Biology*, 2021. Vol. 28. pp. 1024-1032.
**摘要**：首次解析了RelG重组蛋白的2.1Å分辨率晶体结构，发现其N端结构域含有不同于同源蛋白的ATP结合口袋，为设计特异性抑制剂提供了结构依据。
4. **标题**：Functional Analysis of RelG in *Salmonella* Pathogenicity Using Gene Knockout Models
**作者**：Rodríguez, M.E.; Li, X.; Cashel, M.
**期刊**：*PLoS Pathogens*, 2019. Vol. 15. No. 7. e1007953.
**摘要**：通过构建RelG基因缺失的沙门氏菌突变株，发现RelG缺失导致细菌在宿主体内定殖能力显著下降，表明其可能通过调控毒力因子表达影响病原菌致病性。
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**注**：以上文献为模拟示例，实际研究中请以真实发表的论文为准。若需检索真实文献，建议通过PubMed、Web of Science等数据库以“RelG protein”“(p)ppGpp synthase”“stringent response”等关键词组合查询。
**Background of RelG Recombinant Protein**
RelG is a bacterial toxin protein belonging to the toxin-antitoxin (TA) system, specifically categorized as a type II TA module. These systems are widely conserved in prokaryotes and play roles in stress response, biofilm formation, and persister cell formation, which contribute to bacterial survival under adverse conditions. The RelG protein functions as the toxin component, while its cognate antitoxin (RelH) neutralizes its activity under normal conditions. When the antitoxin is degraded during stress, RelG is activated, inhibiting cell growth by targeting essential cellular processes, such as translation or replication.
Recombinant RelG refers to the protein produced through genetic engineering, typically expressed in *E. coli* or other host systems. The gene encoding RelG is cloned into expression vectors, allowing large-scale production for functional and structural studies. Recombinant technology enables purification of RelG in its active form, facilitating research into its mechanisms of action, interaction partners, and potential applications.
Studies on RelG recombinant protein aim to elucidate its role in bacterial physiology and pathogenesis. Its ability to induce dormancy in bacterial populations has implications for understanding antibiotic tolerance and developing strategies to combat persistent infections. Additionally, structural analysis of RelG provides insights into toxin-antitoxin interaction dynamics, aiding in the design of molecules to disrupt TA systems as a novel antimicrobial approach.
Research on RelG also contributes to broader explorations of TA systems as regulatory modules in bacterial evolution and adaptation. The recombinant protein serves as a tool for probing cellular stress pathways and microbial survival mechanisms, with potential applications in biotechnology and therapeutic development.
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