| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | RNU2 |
| Uniprot No | P00654 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-114aa |
| 氨基酸序列 | CDIPQSTNCGGNVYSNDDINTAIQGALDDVANGDRPDNYPHQYYDEASEDITLCCGSGPWSEFPLVYNGPYYSSRDNYVSPGPDRVIYQTNTGEFCATVTHTGAASYDGFTQCS |
| 预测分子量 | 26.4 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RNU2重组蛋白的3篇代表性文献示例(注：文献信息为模拟生成，实际引用需核实数据库)：
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1. **"Reconstitution of the Human U2 snRNP for Functional Splicing Analysis"**
*Lührmann, R., et al.*
摘要：本研究通过体外重组技术成功组装了人源U2 snRNP复合体，验证了核心蛋白(如SF3A/B、U2-A'和U2-B'')在剪接体动态组装中的作用，并证明重组复合体可在体外恢复pre-mRNA剪接活性。
2. **"Structural Insights into U2 snRNP Architecture by Cryo-EM"**
*Nguyen, T.H., et al.*
摘要：利用冷冻电镜解析了重组U2 snRNP的高分辨率结构，揭示了RNU2 RNA与Sm蛋白环的结合模式，并阐明了SF3B1蛋白在靶向剪接位点识别中的构象变化机制。
3. **"RNU2-1 Fragile Site Alterations in Cancer Genomes"**
*Smith, M.J., & Wang, Z.*
摘要：分析了多种癌症中RNU2基因座(2q37.3)的基因组不稳定性，发现其重组蛋白表达异常与剪接失调相关，可能导致肿瘤相关异构体(如BRCA1Δexon9)的异常累积。
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**说明**：
- RNU2是U2 snRNA的基因名称，其重组研究多聚焦于snRNP复合体的体外组装、结构解析或疾病关联。
- 实际文献需在PubMed等平台以关键词“U2 snRNP reconstitution”或“RNU2 splicing”检索，重点关注《Molecular Cell》《Nature Structural Biology》等期刊。
- 技术方法类文献可能涉及重组U2在CRISPR/Cas9适配(如sgRNA改造)中的新兴应用。
建议通过数据库进一步筛选近年高被引论文。
RNU2 recombinant protein is derived from the U2 small nuclear RNA (snRNA), a critical component of the spliceosome machinery essential for pre-mRNA processing in eukaryotic cells. The U2 snRNA, encoded by the RNU2 gene cluster, plays a central role in recognizing the branch site adenosine during spliceosome assembly, enabling precise excision of introns and ligation of exons. Dysregulation of U2 snRNA or its associated proteins has been linked to splicing errors implicated in cancers, neurodegenerative disorders, and genetic diseases.
The recombinant RNU2 protein is typically engineered to study spliceosome dynamics or to model pathological mutations affecting RNA-protein interactions. It is produced by cloning the U2-associated protein-coding sequences into expression vectors (e.g., bacterial or mammalian systems), followed by purification via affinity tagging. This allows researchers to probe structural motifs, such as the Sm protein-binding site or conserved helices critical for base-pairing with pre-mRNA.
Current applications include in vitro splicing assays to dissect mechanistic defects caused by U2 mutations, drug screening for splice-modulating therapeutics, and structural studies using cryo-EM or X-ray crystallography. Challenges remain in maintaining the protein's native conformation post-purification and replicating its dynamic interactions with other spliceosomal components. Ongoing research focuses on leveraging RNU2 recombinant variants to develop antisense oligonucleotides or small molecules targeting splicing anomalies in diseases like spinal muscular atrophy or myelodysplastic syndromes.
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