| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SFRS7 |
| Uniprot No | Q16629 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-238 aa |
| 活性数据 | MSRYGRYGGETKVYVGNLGTGAGKGELERAFSYYGPLRTVWIARNPPGFAFVEFEDPRDAEDAVRGLDGKVICGSRVRVELSTGMPRRSRFDRPPARRPFDPNDRCYECGEKGHYAYDCHRYSRRRRSRSRSRSHSRSRGRRYSRSRSRSRGRRSRSASPRRSRSISLRRSRSASLRRSRSGSIKGSRYFQSPSRSRSRSRSISRPRSSRSKSRSPSPKRSRSPSGSPRRSASPERMD |
| 分子量 | 53.8 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下是关于重组人SFRS7蛋白的3篇参考文献示例(部分为虚构，仅作示例参考)：
---
1. **文献名称**：*Structural insights into the RNA recognition by splicing factor SFRS7*
**作者**：Zhou, Q., Fu, X. D.
**摘要**：该研究解析了SFRS7蛋白的RRM结构域与RNA结合的晶体结构，通过重组表达纯化的SFRS7蛋白揭示了其特异性识别前体mRNA剪接位点的分子机制，阐明了其在剪接体组装中的关键作用。
2. **文献名称**：*SFRS7 overexpression promotes tumorigenesis in glioblastoma via alternative splicing regulation*
**作者**：Lin, Y., et al.
**摘要**：研究利用重组SFRS7蛋白在胶质母细胞瘤细胞系中进行功能实验，发现其过表达通过调控特定癌基因(如EGFR)的可变剪接，增强肿瘤细胞增殖和侵袭能力，提示其作为潜在治疗靶点。
3. **文献名称**：*Phosphorylation-dependent regulation of SFRS7 activity in spliceosome assembly*
**作者**：Xiao, R., et al.
**摘要**：该研究通过体外磷酸化修饰的重组SFRS7蛋白，证明其磷酸化状态动态调控剪接体亚基的招募效率，影响RNA剪接的保真性，并揭示了激酶CLK1在其中的关键作用。
---
注：以上文献名称与作者为示例性质，实际引用时需核实真实发表的论文信息。
Serine/arginine-rich splicing factor 7 (SRSF7), formerly known as SFRS7. is a member of the serine/arginine (SR)-rich protein family involved in constitutive and alternative pre-mRNA splicing. These proteins play critical roles in spliceosome assembly by binding specific exonic or intronic splicing enhancer sequences through their RNA recognition motifs (RRMs), while their RS domains mediate protein-protein interactions essential for splice site selection. SRSF7 is ubiquitously expressed in mammalian cells and regulates the splicing of numerous transcripts linked to cell cycle progression, apoptosis, and DNA repair. It has been implicated in maintaining genome stability and cellular homeostasis, with dysregulation observed in cancers, neurodegenerative disorders, and viral infections.
Recombinant human SRSF7 protein is typically produced using bacterial or eukaryotic expression systems, enabling structural and functional studies. Its recombinant form preserves the modular structure, including the N-terminal RRM for RNA binding and the C-terminal RS domain for interaction with spliceosomal components. Researchers employ recombinant SRSF7 to investigate splicing mechanisms, map protein-RNA interaction networks, and screen small molecules targeting aberrant splicing in diseases. Notably, SRSF7 overexpression correlates with tumor aggressiveness in several cancers, making it a potential therapeutic target. Recent studies also explore its non-canonical roles in mRNA export, translation, and microRNA processing, broadening its significance in post-transcriptional gene regulation.
×
