| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RPL17 |
| Uniprot No | P18621 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-184aa |
| 氨基酸序列 | VRYSLDPENPTKSCKSRGSNLRVHFKNTRETAQAIKGMHIRKATKYLKDVTLQKQCVPFRRYNGGVGRCAQAKQWGWTQGRWPKKSAEFLLHMLKNAESNAELKGLDVDSLVIEHIQVNKAPKMRRRTYRAHGRINPYMSSPCHIEMILTEKEQIVPKPEEEVAQKKKISQKKLKKQKLMARE |
| 预测分子量 | 48.3 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RPL17重组蛋白的3篇参考文献示例(文献信息为虚构示例，仅供格式参考)：
1. **文献名称**：*Cloning and Functional Analysis of Recombinant RPL17 in Ribosome Biogenesis*
**作者**：Smith J, et al.
**摘要**：本研究成功克隆并表达了重组RPL17蛋白，发现其在核糖体大亚基组装中起关键作用，通过体外实验验证了RPL17缺失导致核糖体功能异常。
2. **文献名称**：*Expression and Purification of Human RPL17 Recombinant Protein for Structural Studies*
**作者**：Zhang L, et al.
**摘要**：报道了一种高效表达和纯化人源RPL17重组蛋白的方法，利用X射线晶体学解析其三维结构，揭示了其与rRNA结合的潜在位点。
3. **文献名称**：*RPL17 Recombinant Protein Modulates Cellular Stress Response in Cancer Models*
**作者**：Lee H, et al.
**摘要**：通过体外肿瘤细胞实验，发现重组RPL17蛋白的过表达可抑制内质网应激相关通路，提示其在癌症治疗中的潜在应用价值。
(注：以上文献为假设性示例，实际研究中请通过学术数据库检索具体文献。)
The RPL17 recombinant protein is derived from the ribosomal protein L17 (RPL17), a component of the 60S ribosomal subunit in eukaryotes. Ribosomal proteins like RPL17 are essential for ribosome assembly and protein synthesis, but they also exhibit extraribosomal roles in cellular processes such as DNA repair, apoptosis, and cell cycle regulation. RPL17. encoded by the RPL17 gene, is highly conserved across species, underscoring its fundamental biological importance. Studies have linked dysregulation of RPL17 to various cancers, where its overexpression or mutations may contribute to tumor progression by altering ribosome biogenesis or interacting with oncogenic signaling pathways.
Recombinant RPL17 is produced using genetic engineering techniques, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian or yeast cells) to ensure proper folding and post-translational modifications. The protein is often tagged with markers like His or FLAG for purification and detection. Its production enables functional studies, including structural analysis via X-ray crystallography or cryo-EM, and investigation of its interactions with RNA, other ribosomal proteins, or non-ribosomal partners. Researchers also use recombinant RPL17 to develop antibodies for diagnostic applications or to explore its role in diseases. For instance, in cancer biology, it serves as a potential biomarker or therapeutic target. Additionally, recombinant RPL17 aids in deciphering ribosome assembly mechanisms and understanding how ribosomal dysfunction leads to disorders like ribosomopathies. Its versatility in both basic and applied research highlights its significance in advancing molecular biology and biomedicine.
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