| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | rpl36 |
| Uniprot No | Q6DER2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-105aa |
| 氨基酸序列 | MAIRYPMAVGLNKGHRVTKNVTKPRHCRRRGRLTKHTKFVRDMIREVCGFAPYERRAMELLKVSKDKRALKFIKKRIGTHIRAKRKREELSNVLAAMRKAAAKKD |
| 预测分子量 | 19.8 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RPL36重组蛋白的3篇代表性文献摘要(示例基于研究主题模拟，实际文献需通过数据库验证)：
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1. **文献名称**: *"Cloning and Expression of Recombinant Human RPL36 and Its Role in Ribosome Biogenesis"*
**作者**: Zhang L, et al.
**摘要**: 本研究成功克隆了人类RPL36基因，并在大肠杆菌中高效表达重组蛋白。通过体外核糖体重组实验，发现RPL36对核糖体大亚基的组装具有关键作用，其缺失导致蛋白质翻译效率显著下降。
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2. **文献名称**: *"Structural Characterization of Recombinant RPL36 from Saccharomyces cerevisiae"*
**作者**: Müller S, et al.
**摘要**: 利用X射线晶体学解析了酵母RPL36重组蛋白的三维结构，揭示了其与rRNA结合的特定结构域。研究为理解核糖体L36蛋白在翻译过程中的分子机制提供了结构基础。
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3. **文献名称**: *"RPL36 Recombinant Protein Suppresses Tumor Growth via Modulating p53 Signaling"*
**作者**: Chen H, et al.
**摘要**: 在癌细胞模型中过表达重组RPL36蛋白，发现其通过稳定p53蛋白抑制肿瘤增殖。研究提示RPL36可能作为癌症治疗的潜在靶点，需进一步验证其临床相关性。
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**提示**：建议通过**PubMed**或**Web of Science**检索最新文献(关键词：RPL36 recombinant/expression)，以获取具体实验数据。部分研究可能侧重于RPL36在疾病或代谢通路中的功能，重组蛋白技术常作为基础工具出现。
**Background of RPL36 Recombinant Protein**
Ribosomal protein L36 (RPL36) is a conserved component of the 60S ribosomal subunit, essential for protein synthesis in eukaryotes. As part of the ribosome, RPL36 contributes to the structural stability of the subunit and facilitates the precise alignment of mRNA and tRNA during translation. Beyond its canonical role in translation, emerging studies suggest RPL36 may participate in extraribosomal functions, including cellular stress responses, apoptosis regulation, and interactions with viral or oncogenic proteins, though these roles remain less characterized.
The recombinant RPL36 protein is engineered using heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to enable functional and structural studies. Its recombinant form allows researchers to investigate RPL36’s molecular interactions, post-translational modifications, and potential involvement in diseases. For instance, aberrant expression of ribosomal proteins, including RPL36. has been linked to cancers, such as hepatocellular carcinoma and leukemia, where dysregulated ribosome biogenesis (ribosomopathies) may drive tumorigenesis.
Recombinant RPL36 is particularly valuable for *in vitro* assays, including ribosome assembly reconstitution, binding partner identification (e.g., via pull-down assays), and structural analyses like X-ray crystallography or cryo-EM. Additionally, it serves as an antigen for antibody development to study endogenous protein localization and expression patterns. Recent advances in recombinant protein production, such as codon optimization and fusion tags (e.g., His-tag, GST), have enhanced the solubility and purification efficiency of RPL36. addressing challenges related to its small size (~12 kDa) and potential aggregation.
Overall, RPL36 recombinant protein provides a critical tool for dissecting ribosome biology and exploring its potential as a diagnostic or therapeutic target in diseases linked to translational dysregulation.
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