| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RPL26L1 |
| Uniprot No | Q9UNX3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-145aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMKFNPFV TSDRSKNRKR HFNAPSHVRR KIMSSPLSKE LRQKYNVRSM PIRKDDEVQV VRGHYKGQQI GKVVQVYRKK YVIYIERVQR EKANGTTVHV GIHPSKVVIT RLKLDKDRKK ILERKAKSRQ VGKEKGKYKE ELIEKMQE |
| 预测分子量 | 20 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. |
以下是与RPL26L1重组蛋白相关的参考文献示例(注：内容为模拟概括，实际文献需根据具体研究查询)：
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1. **文献名称**: *RPL26L1 modulates ribosome translation dynamics and promotes p53 activation during DNA damage*
**作者**: Wang Y. et al.
**摘要**: 研究利用重组RPL26L1蛋白揭示其通过结合核糖体RNA调控翻译效率，并在DNA损伤时增强p53信号通路，影响细胞周期停滞和凋亡。
2. **文献名称**: *Recombinant RPL26L1 suppresses tumor growth by inhibiting mTOR signaling in colorectal cancer*
**作者**: Chen L. et al.
**摘要**: 通过体外表达RPL26L1重组蛋白，发现其能竞争性抑制mTORC1复合物的形成，从而抑制结直肠癌细胞增殖并诱导自噬。
3. **文献名称**: *Structural insights into RPL26L1’s role in ribosome biogenesis using cryo-EM*
**作者**: Gupta S. et al.
**摘要**: 利用重组RPL26L1蛋白进行冷冻电镜分析，揭示其与核糖体大亚基结合的构象变化，为核糖体组装异常相关疾病的机制提供依据。
4. **文献名称**: *RPL26L1 recombinant protein as a potential biomarker for hepatocellular carcinoma diagnosis*
**作者**: Kim H. et al.
**摘要**: 研究显示肝癌患者血清中RPL26L1重组蛋白水平显著升高，可能通过调控Wnt/β-catenin通路促进肿瘤侵袭，提示其作为诊断标志物的潜力。
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建议通过PubMed、Web of Science等平台用关键词“RPL26L1 recombinant”或“RPL26L1 protein”检索最新文献以获取准确信息。
The RPL26L1 recombinant protein is derived from the ribosomal protein L26-like 1 (RPL26L1), a member of the L26 family of ribosomal proteins. Unlike its homolog RPL26. which is ubiquitously expressed and integral to ribosome assembly and translation, RPL26L1 exhibits tissue-specific expression, with higher levels observed in immune cells, testes, and certain cancers. This divergence suggests distinct regulatory roles beyond canonical protein synthesis, potentially influencing cellular processes like proliferation, differentiation, or stress responses.
RPL26L1 shares ~60% amino acid sequence identity with RPL26. but differences in its C-terminal region may confer unique interactions with RNA or other ribosomal components. Studies indicate RPL26L1 might participate in extraribosomal functions, including modulating mRNA stability or acting as a signaling intermediate. Its overexpression in malignancies such as hepatocellular carcinoma and glioblastoma has sparked interest in its oncogenic potential, though mechanistic insights remain limited.
Recombinant RPL26L1 is typically produced via heterologous expression systems (e.g., E. coli or mammalian cells) for functional studies. Purified proteins enable in vitro analyses of RNA-binding properties, protein-protein interactions, and structural characterization. Researchers also employ it to investigate competitive binding with RPL26. explore its role in specialized ribosome populations, or develop antibodies for diagnostic applications.
Current research focuses on elucidating RPL26L1's contributions to cellular adaptation, disease progression, and its potential as a therapeutic target. The recombinant protein serves as a critical tool for dissecting these biological questions while minimizing confounding factors from endogenous cellular environments.
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