| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RBM17 |
| Uniprot No | Q96I25 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-401aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSLYDDLGVETSDSKTEGWSKNFKLLQSQL QVKKAALTQAKSQRTKQSTVLAPVIDLKRGGSSDDRQIVDTPPHVAAGLK DPVPSGFSAGEVLIPLADEYDPMFPNDYEKVVKRQREERQRQRELERQKE IEEREKRRKDRHEASGFARRPDPDSDEDEDYERERRKRSMGGAAIAPPTS LVEKDKELPRDFPYEEDSRPRSQSSKAAIPPPVYEEQDRPRSPTGPSNSF LANMGGTVAHKIMQKYGFREGQGLGKHEQGLSTALSVEKTSKRGGKIIVG DATEKDASKKSDSNPLTEILKCPTKVVLLRNMVGAGEVDEDLEVETKEEC EKYGKVGKCVIFEIPGAPDDEAVRIFLEFERVESAIKAVVDLNGRYFGGR VVKACFYNLDKFRVLDLAEQV |
| 预测分子量 | 47 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RBM17重组蛋白的3篇参考文献示例(基于公开研究主题概括，非真实文献)：
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1. **文献名称**: *RBM17 interacts with spliceosomal components and regulates alternative splicing in cancer cells*
**作者**: Smith J, et al.
**摘要**: 本研究通过重组RBM17蛋白的体外结合实验，证明其与U2 snRNP复合物相互作用，调控肿瘤细胞中BCL2L1等基因的可变剪接，促进细胞存活。
2. **文献名称**: *Functional characterization of recombinant RBM17 in RNA recognition and splicing regulation*
**作者**: Lee S, et al.
**摘要**: 利用重组RBM17蛋白进行RNA pull-down实验，揭示其通过N端的RNA结合结构域识别特定RNA序列，并在神经细胞分化中调控剪接因子相互作用。
3. **文献名称**: *RBM17 deficiency alters DNA damage response via impaired spliceosome assembly*
**作者**: Zhang Y, et al.
**摘要**: 通过重组RBM17蛋白的体外剪接活性分析，发现其缺失导致BRCA1等DNA修复基因的异常剪接，影响同源重组修复通路。
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**备注**：以上文献为示例，实际研究中建议通过PubMed或Web of Science以“RBM17 recombinant protein”或“RBM17 splicing function”为关键词检索近期论文。
RBM17 (RNA Binding Motif Protein 17) is a splicing factor belonging to the serine/arginine (SR)-rich family of proteins, which play critical roles in pre-mRNA splicing—a process essential for gene expression regulation. It contains an N-terminal RNA recognition motif (RRM) and a C-terminal domain enriched in serine and arginine residues, characteristic of proteins involved in spliceosome assembly. RBM17 interacts with components of the core splicing machinery, including U2AF65 and SF3b, facilitating recognition of splice sites and influencing alternative splicing decisions. Dysregulation of RBM17 has been implicated in diseases such as cancer, where aberrant splicing contributes to tumor progression and metastasis. For instance, studies suggest RBM17 overexpression promotes oncogenic splicing events in lung adenocarcinoma and hepatocellular carcinoma. Recombinant RBM17 proteins are typically produced using bacterial (e.g., *E. coli*) or mammalian expression systems, enabling biochemical studies of its RNA-binding properties, spliceosomal interactions, and structural analysis. These recombinant tools are vital for dissecting RBM17's molecular mechanisms, screening splicing-modulating compounds, and exploring its role as a potential therapeutic target. Recent structural studies using recombinant RBM17 have begun to elucidate how its RRM domain recognizes specific RNA motifs, providing insights into splicing fidelity. However, its precise regulatory networks and context-dependent functions in development and disease remain areas of active research.
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