| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | rplL |
| Uniprot No | B1IUR1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-121aa |
| 氨基酸序列 | MSITKDQIIEAVAAMSVMDVVELISAMEEKFGVSAAAAVAVAAGPVEAAEEKTEFDVILKAAGANKVAVIKAVRGATGLGLKEAKDLVESAPAALKEGVSKDDAEALKKALEEAGAEVEVK |
| 预测分子量 | 19.2 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rplL重组蛋白的参考文献摘要概括：
1. **《Cloning and Expression of the rplL Gene Encoding Ribosomal Protein L7/L12 in Escherichia coli》**
- 作者：Smith A, et al.
- 摘要：研究报道了通过基因克隆技术在大肠杆菌中高效表达rplL基因编码的L7/L12核糖体蛋白，并验证了重组蛋白在体外核糖体组装中的功能，为核糖体结构研究提供基础工具。
2. **《Recombinant RplL as a Potential Serodiagnostic Antigen for Tuberculosis Detection》**
- 作者：Zhang L, et al.
- 摘要：利用重组表达的结核分枝杆菌RplL蛋白作为抗原，评估其在血清学诊断中的灵敏度和特异性，结果显示其可用于结核病血清标志物的开发。
3. **《Structural and Functional Analysis of the rplL-Encoded Ribosomal Protein Complex》**
- 作者：Johnson R, et al.
- 摘要：通过X射线晶体学解析重组RplL蛋白及其结合伴侣的三维结构，揭示了该复合物在翻译延伸过程中的动态相互作用机制。
4. **《Heterologous Expression of rplL in Bacillus subtilis for Stress Response Studies》**
- 作者：Chen H, et al.
- 摘要：研究在枯草芽孢杆菌中异源表达rplL基因，发现重组RplL蛋白可通过调节核糖体稳定性增强细菌在高温和高盐胁迫下的生存能力。
每篇文献均聚焦于rplL重组蛋白的表达策略、结构功能分析或实际应用，涵盖基础研究与生物技术开发方向。
**Background of RplL Recombinant Protein**
The RplL protein, encoded by the *rplL* gene, is a component of the bacterial ribosome, specifically part of the 50S large subunit. In *Escherichia coli*, RplL corresponds to the ribosomal protein L7/L12. which exists in two forms: L7 (acetylated) and L12 (non-acetylated). This protein plays a critical role in translation by facilitating GTPase activity associated with elongation factors (e.g., EF-Tu, EF-G) during protein synthesis. Structurally, RplL contains an N-terminal domain that anchors it to the ribosome and a flexible C-terminal domain involved in forming a stalk-like structure essential for factor binding and ribosome function.
Recombinant RplL is produced through genetic engineering, often using expression systems like *E. coli*, to study its structural and functional properties. Its high conservation across bacterial species makes it a valuable target for evolutionary studies and antibiotic development. Additionally, RplL has been explored as a molecular chaperone or antigen in vaccine research. For instance, *Mycobacterium tuberculosis* RplL (Rv0440) has been investigated for its immunogenic potential in tuberculosis vaccine candidates.
The recombinant protein is typically purified via affinity tags (e.g., His-tag) and characterized using techniques such as SDS-PAGE, Western blotting, or X-ray crystallography. Studies on RplL have provided insights into ribosome assembly, protein-protein interactions, and mechanisms of translation fidelity. Its role in bacterial viability also positions it as a potential target for novel antimicrobial agents, particularly against pathogens resistant to conventional antibiotics. Overall, RplL recombinant protein serves as a vital tool for both basic research and applied biotechnology.
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