| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RpL10 |
| Uniprot No | P27635 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-214aa |
| 氨基酸序列 | MGRRPARCYRYCKNKPYPKSRFCRGVPDAKIRIFDLGRKKAKVDEFPLCGHMVSDEYEQLSSEALEAARICANKYMVKSCGKDGFHIRVRLHPFHVIRINKMLSCAGADRLQTGMRGAFGKPQGTVARVHIGQVIMSIRTKLQNKEHVIEALRRAKFKFPGRQKIHISKKWGFTKFNADEFEDMVAEKRLIPDGCGVKYIPSRGPLDKWRALHS |
| 预测分子量 | 24,5 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RPL10重组蛋白的3篇代表性文献摘要(文献标题与内容为示例性概括，具体引用时请核实原文)：
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1. **文献名称**: "Structural and functional analysis of recombinant human RPL10 in ribosome assembly"
**作者**: Smith A, et al.
**摘要**: 本研究通过大肠杆菌表达系统成功纯化了重组人源RPL10蛋白，并利用X射线晶体学解析其三维结构。研究发现RPL10在核糖体大亚基组装中通过特定结构域与RNA相互作用，突变其保守区域会破坏核糖体功能。
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2. **文献名称**: "RPL10 mutations alter recombinant protein stability and link to autism spectrum disorders"
**作者**: Lee B, et al.
**摘要**: 文章分析了自闭症患者中发现的RPL10点突变(如H213Q)对重组蛋白稳定性的影响。通过体外实验表明，突变体RPL10重组蛋白更易被蛋白酶降解，导致核糖体功能异常，可能通过干扰mTOR信号通路参与神经发育障碍。
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3. **文献名称**: "Recombinant RPL10 suppresses T-ALL progression by modulating oncogenic mRNA translation"
**作者**: Chen X, et al.
**摘要**: 研究团队利用昆虫细胞表达系统制备了高纯度重组RPL10蛋白，发现其在T细胞急性淋巴细胞白血病(T-ALL)模型中可竞争性抑制突变型RPL10的异常核糖体结合，从而选择性阻断癌基因(如c-MYC)的翻译，抑制肿瘤生长。
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**备注**：以上内容为领域研究方向示例，实际文献需通过PubMed或Google Scholar检索关键词(如"RPL10 recombinant"、"RPL10 expression purification")获取。近年研究多聚焦于RPL10突变与疾病关联及重组蛋白的功能验证。
**Background of Recombinant RpL10 Protein**
Ribosomal protein L10 (RpL10), also known as L10e or uL16. is a conserved component of the 60S large ribosomal subunit in eukaryotes. It plays a critical role in ribosome biogenesis, translation, and the assembly of functional ribosomal complexes. Structurally, RpL10 contains distinct domains that mediate interactions with rRNA and other ribosomal proteins, contributing to the stability and catalytic activity of the ribosome. Beyond its canonical role in protein synthesis, RpL10 has been implicated in extra-ribosomal functions, including cell cycle regulation, apoptosis, and signaling pathways, such as the NF-κB and mTOR networks.
Recombinant RpL10 is engineered using expression systems like *E. coli* or yeast to produce high-purity, functional protein for research. This approach overcomes challenges in isolating native RpL10 from cellular sources, which is often low in abundance or entangled with ribosomal complexes. The recombinant protein typically includes affinity tags (e.g., His-tag) for simplified purification and detection.
Studies leveraging recombinant RpL10 have advanced understanding of ribosome structure (via cryo-EM or X-ray crystallography) and translation mechanisms. Mutational analyses have identified residues critical for ribosome assembly or interactions with cofactors like MDM2. a regulator linked to cancer. Dysregulation of RpL10 is associated with diseases, including Diamond-Blackfan anemia and certain cancers, highlighting its potential as a therapeutic target.
Ongoing research explores RpL10’s role in cellular stress responses, viral replication (e.g., interactions with viral RNA), and its emerging connection to neurodevelopmental disorders. Recombinant RpL10 remains a vital tool for dissecting ribosomal functions and developing targeted therapies.
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