| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SRSF9 |
| Uniprot No | Q13242 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-221aa |
| 氨基酸序列 | MSGWADERGGEGDGRIYVGNLPTDVREKDLEDLFYKYGRIREIELKNRHGLVPFAFVRFEDPRDAEDAIYGRNGYDYGQCRLRVEFPRTYGGRGGWPRGGRNGPPTRRSDFRVLVSGLPPSGSWQDLKDHMREAGDVCYADVQKDGVGMVEYLRKEDMEYALRKLDDTKFRSHEGETSYIRVYPERSTSYGYSRSRSGSRGRDSPYQSRGSPHYFSPFRPY |
| 预测分子量 | 52.5 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SRSF9重组蛋白的3篇模拟参考文献(基于领域研究背景整理，非真实文献)：
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1. **文献名称**: *"Recombinant SRSF9 protein regulates alternative splicing in vitro by binding exonic motifs"*
**作者**: Li, X. et al.
**摘要**: 研究通过原核表达系统纯化重组人SRSF9蛋白，发现其通过结合靶RNA外显子区域的富嘌呤序列，调控前体mRNA的剪接位点选择。体外剪接实验表明，SRSF9缺失会导致特定基因(如CASP9)的促凋亡异构体增加。
2. **文献名称**: *"SRSF9 recombinant protein suppresses viral replication by enhancing antiviral mRNA stability"*
**作者**: Chen, H. & Wang, R.
**摘要**: 该研究利用哺乳动物细胞表达系统获得重组SRSF9蛋白，发现其通过结合病毒RNA的3'非翻译区(3'UTR)，增强宿主抗病毒mRNA(如IFN-β)的稳定性，从而抑制RNA病毒(如流感病毒)的复制。
3. **文献名称**: *"Structural analysis of SRSF9 RRM domains and their impact on RNA recognition"*
**作者**: Gupta, S. et al.
**摘要**: 通过重组表达SRSF9的RNA识别基序(RRM)结构域，结合X射线晶体学分析，揭示其与RNA结合的分子机制，并发现磷酸化修饰(如Serine 100)可动态调节其RNA结合能力，影响剪接效率。
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**备注**：以上文献为模拟示例，实际研究需通过PubMed、Web of Science等平台检索真实文献(关键词：SRSF9 recombinant protein/splicing/RNA binding)。
SRSF9 (Serine/Argınine-Rich Splicing Factor 9) is a member of the SR protein family, a group of essential regulators of constitutive and alternative pre-mRNA splicing. These proteins play critical roles in spliceosome assembly, exon recognition, and splice site selection by interacting with RNA and other splicing factors. SRSF9 contains characteristic structural motifs, including RNA recognition motifs (RRMs) for binding specific RNA sequences and a serine/arginine-rich (RS) domain for protein-protein interactions. It is ubiquitously expressed in human tissues and localized primarily in the nucleus.
Recombinant SRSF9 protein is produced using engineered expression systems (e.g., E. coli or mammalian cells) to study its molecular functions. Purified recombinant SRSF9 retains RNA-binding activity and can modulate splicing events in vitro, making it a valuable tool for dissecting splicing mechanisms. Studies have shown that SRSF9 regulates alternative splicing of transcripts involved in cell cycle control, apoptosis, and stress responses. Dysregulation of SRSF9 has been implicated in cancers, including glioblastoma and hepatocellular carcinoma, where its overexpression correlates with tumor progression and poor prognosis. Additionally, it interacts with viral RNAs and proteins, potentially influencing viral replication pathways (e.g., HIV-1).
Researchers use recombinant SRSF9 to investigate post-translational modifications (e.g., phosphorylation) that regulate its activity, its interplay with other splicing factors (e.g., SRSF1/SRSF2), and its role in disease-associated splicing errors. Its recombinant form is also employed in high-throughput screens to identify small molecules targeting aberrant splicing in cancer or viral infections. Ongoing research aims to clarify its tissue-specific functions and therapeutic potential.
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