| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RPL9 |
| Uniprot No | P32969 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-192aa |
| 氨基酸序列 | MKTILSNQTVDIPENVDITLKGRTVIVKGPRGTLRRDFNHINVELSLLGKKKKRLRVDKWWGNRKELATVRTICSHVQNMIKGVTLGFRYKMRSVYAHFPINVVIQENGSLVEIRNFLGEKYIRRVRMRPGVACSVSQAQKDELILEGNDIELVSNSAALIQQATTVKNKDIRKFLDGIYVSEKGTVQQADE |
| 预测分子量 | 48.9 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. |
以下是模拟生成的3篇关于RPL9重组蛋白的参考文献示例(注：实际文献需通过学术数据库查询，以下内容仅供格式参考)：
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1. **标题**: *"Recombinant RPL9 Expression in E. coli: Purification and Structural Characterization"*
**作者**: Smith J, et al.
**摘要**: 本研究报道了通过大肠杆菌系统高效表达重组人源RPL9蛋白的优化方法，采用His标签纯化获得高纯度蛋白，并通过圆二色光谱验证其二级结构完整性，为后续功能研究奠定基础。
2. **标题**: *"RPL9 Regulates p53-dependent Apoptosis in Cancer Cells via Ribosome Stress Signaling"*
**作者**: Chen L, et al.
**摘要**: 发现重组RPL9蛋白的异常表达可激活核糖体应激通路，通过p53依赖的机制诱导癌细胞凋亡，提示RPL9在肿瘤治疗中的潜在靶点价值。
3. **标题**: *"Cryo-EM Analysis of Recombinant RPL9 Reveals Its Role in Ribosomal Subunit Assembly"*
**作者**: Müller S, et al.
**摘要**: 利用冷冻电镜解析重组RPL9与28S rRNA的复合物结构，阐明其在核糖体大亚基组装过程中的关键相互作用位点，为遗传性核糖体病机制提供新见解。
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**建议**：实际文献请通过PubMed、Web of Science等平台，以关键词“recombinant RPL9”、“RPL9 protein expression”检索，并筛选近五年高被引研究。
Ribosomal protein L9 (RPL9) is a component of the 60S large ribosomal subunit, playing a structural and functional role in protein synthesis. As part of the ribosome, it contributes to the stabilization of rRNA tertiary interactions and facilitates proper ribosome assembly. Beyond its canonical role in translation, RPL9 has been implicated in extra-ribosomal functions, including cellular stress responses, apoptosis regulation, and interactions with viral or oncogenic proteins. Its conserved structure features a unique two-domain architecture: an N-terminal globular domain and an extended C-terminal α-helix, which spans the ribosome’s subunit interface.
Recombinant RPL9 is produced using expression systems like *E. coli* or mammalian cells, often fused with affinity tags (e.g., His-tag) for purification. Its recombinant form enables studies on ribosome biogenesis, translation mechanisms, and disease associations. Dysregulation of RPL9 has been linked to cancers, such as colorectal and hepatocellular carcinoma, where it may act as a biomarker or therapeutic target. Researchers also employ recombinant RPL9 to investigate its interactions with antibiotics or antiviral compounds, aiding drug development.
Challenges in RPL9 recombinant production include maintaining solubility and proper folding due to its elongated structure. Optimization of expression conditions (e.g., low temperature, codon usage adaptation) or co-expression with chaperones is often required. Validated through techniques like Western blot, circular dichroism, or functional assays, recombinant RPL9 serves as a critical tool for deciphering ribosome-related pathologies and molecular biology mechanisms.
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