| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RPL13 |
| Uniprot No | P26373 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-211 aa |
| 活性数据 | MAPSRNGMVL KPHFHKDWQR RVATWFNQPA RKIRRRKARQ AKARRIAPRP ASGPIRPIVR CPTVRYHTKV RAGRGFSLEE LRVAGIHKKV ARTIGISVDP RRRNKSTESL QANVQRLKEY RSKLILFPRK PSAPKKGDSS AEELKLATQL TGPVMPVRNV YKKEKARVIT EEEKNFKAFA SLRMARANAR LFGIRAKRAK EAAEQDVEKK K |
| 分子量 | 24.2 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. |
以下是三篇关于人RPL13蛋白的示例参考文献及简要摘要(注：以下文献为根据研究领域撰写的示例，非真实文献)：
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1. **文献名称**：*RPL13 phosphorylation regulates its role in inflammatory gene expression*
**作者**：Smith A. et al.
**摘要**：研究发现，在炎症刺激下(如IL-1β)，RPL13从核糖体解离并被磷酸化，随后与趋化因子(如CCL5)mRNA结合，调控其翻译，揭示RPL13作为核糖体蛋白在炎症反应中的双重功能。
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2. **文献名称**：*Crystal structure of human ribosomal protein L13 reveals key functional domains*
**作者**：Zhang L. et al.
**摘要**：通过解析重组人RPL13蛋白的晶体结构，确定了其RNA结合域和与其他核糖体蛋白(如RPL11)的相互作用界面，为研究核糖体组装异常相关疾病(如Diamond-Blackfan贫血)提供结构基础。
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3. **文献名称**：*RPL13 acts as a tumor suppressor by interacting with p53-MDM2 pathway*
**作者**：Chen H. et al.
**摘要**：在乳腺癌细胞中，RPL13过表达通过稳定p53蛋白并抑制MDM2介导的降解，诱导细胞周期阻滞和凋亡，提示RPL13可作为癌症治疗的潜在靶点。
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(若需扩展文献范围，可补充RPL13与核糖体应激、自身免疫疾病相关的研究方向。)
Recombinant human RPL13 (Ribosomal Protein L13) is a key component of the 60S ribosomal subunit, playing a critical role in protein synthesis by facilitating ribosome assembly and translational fidelity. As part of the ribosomal protein family, RPL13 contributes to the structural stability of ribosomes and participates in the formation of the peptidyl transferase center. Beyond its canonical role in translation, RPL13 has been implicated in extraribosomal functions, including the regulation of cellular stress responses, inflammation, and apoptosis. For instance, it is part of the interferon-γ-activated inhibitor of translation (GAIT) complex, which modulates mRNA translation under inflammatory conditions.
Recombinant RPL13 is typically expressed in bacterial or eukaryotic systems (e.g., *E. coli* or mammalian cells) using genetic engineering techniques, enabling high-purity yields for biochemical studies. Its recombinant form retains structural and functional integrity, allowing researchers to investigate interactions with RNA, proteins, or small molecules. This has proven valuable in studying diseases linked to ribosomal dysfunction, such as cancer, Diamond-Blackfan anemia, and neurodegenerative disorders. Additionally, recombinant RPL13 serves as a standard in proteomics, diagnostic assays, and therapeutic development, particularly in targeting pathways involving translational dysregulation. Ongoing research continues to unravel its dual roles in ribosome-dependent and independent processes, highlighting its potential as a biomarker or therapeutic target.
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