| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SRSF3 |
| Uniprot No | P84103 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-85aa |
| 氨基酸序列 | MHRDSCPLDCKVYVGNLGNNGNKTELERAFGYYGPLRSVWVARNPPGFAF VEFEDPRDAADAVRELDGRTLCGCRVRVELSNGEK |
| 预测分子量 | 35 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. |
1. **"Recombinant SRSF3 expression and its role in alternative splicing regulation"**
- 作者: Li, X. et al.
- 摘要：研究通过大肠杆菌系统表达重组SRSF3蛋白，验证其在体外剪接实验中对靶基因(如Caspase-9)可变剪接的调控作用，揭示其通过结合特定RNA基序影响剪接体组装。
2. **"Structural insights into SRSF3 RNA recognition motif using recombinant protein crystallography"**
- 作者: Zhang, Y. & Wang, H.
- 摘要：利用重组SRSF3蛋白进行X射线晶体学分析，解析其RNA结合结构域(RRM)的三维结构，阐明其与pre-mRNA中保守序列的相互作用机制。
3. **"SRSF3 recombinant protein suppresses viral replication by modulating host splicing machinery"**
- 作者: Kim, S. et al.
- 摘要：研究重组SRSF3蛋白在抗病毒反应中的作用，发现其通过干扰病毒RNA剪接(如HIV-1)抑制病毒复制，为抗病毒治疗提供新靶点。
4. **"Purification and functional analysis of SRSF3 recombinant protein in cancer cell proliferation"**
- 作者: Chen, L. et al.
- 摘要：通过杆状病毒-昆虫细胞系统纯化重组SRSF3.证明其在肝癌细胞中过表达可促进增殖相关剪接事件(如MYC异构体)，揭示其促癌机制。
(注：上述文献信息为示例虚构，实际需根据具体研究检索PubMed等数据库获取。)
SRSF3 (serine/arginine-rich splicing factor 3), also known as SRp20. is a critical member of the serine/arginine (SR) protein family involved in constitutive and alternative pre-mRNA splicing. It plays a multifaceted role in post-transcriptional gene regulation, including mRNA export, translation, and genome stability. Structurally, SRSF3 contains an N-terminal RNA recognition motif (RRM) for binding exonic splicing enhancer sequences and a C-terminal RS domain rich in serine/arginine dipeptides, which mediates protein-protein interactions and subcellular localization.
This protein is essential for cell cycle progression, proliferation, and apoptosis. Studies highlight its dual role as both a proto-oncogene and tumor suppressor, depending on cellular context. Overexpression of SRSF3 is linked to cancers such as hepatocellular carcinoma and breast cancer, where it promotes aberrant splicing of genes involved in metastasis and drug resistance. Conversely, its downregulation correlates with genomic instability and impaired DNA repair.
Recombinant SRSF3 proteins are typically produced in *E. coli* or mammalian expression systems, often fused with tags like His-tag or GST for purification. These tools enable mechanistic studies of splicing regulation, identification of RNA-binding targets via CLIP-seq, and screening for splicing-modulating compounds. Researchers also use recombinant SRSF3 to rescue cellular phenotypes in knockout models or to explore isoform-specific functions in disease.
Despite its well-characterized roles, questions remain about its context-dependent regulatory networks and therapeutic targeting potential. Ongoing research focuses on elucidating how post-translational modifications (e.g., phosphorylation) fine-tune its activity in stress responses and carcinogenesis.
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