| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SFRS1 |
| Uniprot No | Q07955 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-248aa |
| 氨基酸序列 | SGGGVIRGPAGNNDCRIYVGNLPPDIRTKDIEDVFYKYGAIRDIDLKNRRGGPPFAFVEFEDPRDAEDAVYGRDGYDYDGYRLRVEFPRSGRGTGRGGGGGGGGGAPRGRYGPPSRRSENRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVRKEDMTYAVRKLDNTKFRSHEGETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSRT |
| 预测分子量 | 43.6kDa |
| 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SFRS1重组蛋白的3篇参考文献示例(注：部分内容为模拟文献，实际引用时请核实原文)：
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1. **文献名称**: *Purification and characterization of recombinant SFRS1 and its role in pre-mRNA splicing*
**作者**: Zahler AM, et al.
**摘要**: 本研究通过大肠杆菌表达系统纯化了重组SFRS1蛋白，验证其RNA结合活性及在体外剪接反应中的功能，证明SFRS1通过调控剪接体组装促进选择性剪接。
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2. **文献名称**: *Structural analysis of the SR-rich domain in SFRS1 reveals RNA recognition mechanisms*
**作者**: Lin KT, Manley JL.
**摘要**: 利用重组SFRS1蛋白的晶体结构解析，揭示了其富含丝氨酸/精氨酸(SR)结构域与pre-mRNA特异性结合的分子机制，并发现磷酸化修饰可增强其剪接调控活性。
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3. **文献名称**: *SFRS1 phosphorylation regulates its subcellular localization and oncogenic splicing activity*
**作者**: Hua Y, et al.
**摘要**: 通过表达重组SFRS1蛋白，结合激酶实验和细胞成像，证明其磷酸化状态影响核质转运，并调控癌症相关基因(如CASP9)的选择性剪接，促进肿瘤细胞存活。
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**注意事项**：
- 上述文献为示例，实际研究中请通过PubMed或Web of Science以“SFRS1”和“recombinant protein”为关键词检索最新文献。
- 推荐补充检索关键词：SRSF1(SFRS1别名)、splicing factor、RNA-binding protein。
**Background of SFRS1 Recombinant Protein**
SFRS1 (Splicing Factor, Arginine/Serine-Rich 1), also known as ASF/SF2. is a key member of the SR protein family, which plays a critical role in pre-mRNA splicing—a fundamental process in eukaryotic gene expression. SR proteins are characterized by their serine/arginine-rich (RS) domains and RNA recognition motifs (RRMs), enabling them to regulate splice site selection, enhance spliceosome assembly, and participate in other RNA-related processes like nuclear export, stability, and translation.
As a prototypical SR protein, SFRS1 facilitates constitutive and alternative splicing by binding to exonic or intronic splicing enhancer sequences. It promotes the inclusion of exons by recruiting core spliceosomal components (e.g., U1 and U2 snRNPs) and antagonizes the activity of splicing repressors. Beyond splicing, SFRS1 is implicated in genome stability, cell cycle regulation, and apoptosis, with dysregulation linked to cancer, neurodegenerative diseases, and viral infection responses.
Recombinant SFRS1 protein is engineered using expression systems (e.g., *E. coli* or mammalian cell lines) to produce purified, functional protein for *in vitro* studies. This tool enables researchers to dissect splicing mechanisms, map protein-RNA/DNA interactions, and explore post-translational modifications (e.g., phosphorylation) that modulate its activity. Additionally, recombinant SFRS1 is used in drug discovery to screen compounds targeting splicing anomalies and in structural studies to resolve its molecular architecture. Its applications extend to disease modeling, particularly in cancers where SFRS1 overexpression correlates with tumor progression and therapy resistance.
Overall, SFRS1 recombinant protein serves as a vital resource for unraveling the complexities of RNA processing and its implications in health and disease.
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