| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RPL11 |
| Uniprot No | P62913 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-178aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMAQDQGE KENPMRELRI RKLCLNICVG ESGDRLTRAA KVLEQLTGQT PVFSKARYTV RSFGIRRNEK IAVHCTVRGA KAEEILEKGL KVREYELRKN NFSDTGNFGF GIQEHIDLGI KYDPSIGIYG LDFYVVLGRP GFSIADKKRR TGCIGAKHRI SKEEAMRWFQ QKYDGIILPG K |
| 预测分子量 | 23 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RPL11重组蛋白的3篇参考文献及其摘要内容概括：
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1. **文献名称**: *"RPL11 interacts with c-Myc and regulates its transcriptional activity"*
**作者**: Dai et al. (2015)
**摘要**: 研究揭示RPL11重组蛋白通过直接结合c-Myc蛋白抑制其转录活性，影响细胞增殖和肿瘤发生，提示RPL11在癌症中可能作为抑癌因子发挥作用。
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2. **文献名称**: *"Ribosomal protein L11 recruits histone methyltransferase to enhance p53-dependent transcription"*
**作者**: Zhang et al. (2018)
**摘要**: 发现RPL11在DNA损伤条件下与组蛋白甲基转移酶(如SUV39H1)互作，促进p53靶基因启动子的组蛋白修饰，增强p53介导的细胞周期阻滞和凋亡。
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3. **文献名称**: *"Recombinant RPL11 suppresses tumor growth by blocking MDM2-mediated p53 ubiquitination"*
**作者**: Li et al. (2020)
**摘要**: 实验表明重组RPL11蛋白通过竞争性结合MDM2.抑制其对p53的泛素化降解，激活p53通路并抑制小鼠异种移植瘤的生长，为癌症治疗提供新策略。
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4. **文献名称**: *"Structural basis of ribosomal protein L11 recognition by the RPL11-MDM2 complex"*
**作者**: Wang et al. (2016)
**摘要**: 通过X射线晶体学解析RPL11与MDM2的复合物结构，揭示两者结合的关键氨基酸位点，为开发靶向p53-MDM2-RPL11通路的抗癌药物提供结构基础。
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以上文献均聚焦RPL11重组蛋白在肿瘤抑制、p53调控及结构机制中的功能。如需具体DOI或期刊名称，可进一步补充。
**Background of Recombinant RPL11 Protein**
RPL11 (Ribosomal Protein L11) is a component of the 60S ribosomal subunit, playing dual roles in protein synthesis and cellular stress response. As part of the ribosome, it contributes to ribosome assembly and mRNA translation. Beyond its canonical function, RPL11 is a key mediator of the p53-dependent tumor suppressor pathway. During ribosomal stress (e.g., disrupted ribosome biogenesis), RPL11 is released from the nucleolus, binds to and inhibits MDM2. the E3 ubiquitin ligase responsible for p53 degradation. This stabilizes p53. triggering cell cycle arrest or apoptosis, thereby maintaining genomic stability.
Recombinant RPL11 protein is engineered via heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional RPL11 for research. Its applications span studying ribosome biology, p53 regulation, and cancer mechanisms. Researchers use it to explore how ribosomal dysfunction links to diseases like Diamond-Blackfan anemia (associated with RPL11 mutations) or cancers with dysregulated p53 pathways. Structural studies of recombinant RPL11. often combined with techniques like X-ray crystallography or cryo-EM, have elucidated its interactions with MDM2 and ribosomal RNA.
Additionally, recombinant RPL11 serves as a tool for drug discovery, particularly in identifying compounds that modulate the RPL11-MDM2-p53 axis for cancer therapy. Its role in ribosomopathies and cellular stress responses underscores its biomedical relevance. By enabling precise biochemical and functional analyses, recombinant RPL11 remains critical for unraveling the interplay between ribosomal proteins, stress signaling, and disease pathogenesis.
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