| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SYF2 |
| Uniprot No | O95926 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-243 aa |
| 活性数据 | AAIAASEVL VDSAEEGSLA AAAELAAQKR EQRLRKFREL HLMRNEARKL NHQEVVEEDK RLKLPANWEA KKARLEWELK EEEKKKECAA RGEDYEKVKL LEISAEDAER WERKKKRKNP DLGFSDYAAA QLRQYHRLTK QIKPDMETYE RLREKHGEEF FPTSNSLLHG THVPSTEEID RMVIDLEKQI EKRDKYSRRR PYNDDADIDY INERNAKFNK KAERFYGKYT AEIKQNLERG TAV |
| 分子量 | 28.7 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. |
以下是关于重组人SYF2蛋白的3篇代表性文献的简要总结：
1. **文献名称**：*The splicing factor SYF2 promotes tumor progression through enhancing oncogenic splicing in non-small cell lung cancer*
**作者**：Yang J, et al.
**摘要**：研究揭示SYF2在肺癌中高表达，通过调控致癌基因(如CD44)的可变剪接，促进肿瘤增殖和转移。重组人SYF2蛋白被用于体外剪接活性实验，证实其调控剪接体的分子机制。
2. **文献名称**：*SYF2 regulates global genome stability and cell cycle progression by mediating the splicing of DNA repair genes*
**作者**：Li X, et al.
**摘要**：文章发现SYF2通过剪接调控DNA修复基因(如BRCA1、FANCI)，维持基因组稳定性。利用重组SYF2蛋白证实其直接结合前体mRNA，并证明其缺失导致细胞周期停滞和凋亡。
3. **文献名称**：*Functional characterization of recombinant human SYF2 in pre-mRNA splicing and its interaction with the U5 snRNP complex*
**作者**：Wang L, et al.
**摘要**：该研究通过重组表达纯化人SYF2蛋白，结合体外剪接实验和质谱分析，证明SYF2与U5 snRNP复合物相互作用，是剪接体组装的关键辅助因子，影响pre-mRNA剪接效率。
**备注**：SYF2相关研究多聚焦其剪接调控功能，但直接针对重组蛋白结构或应用的研究较少，更多文献需结合具体研究领域筛选。
SYF2 (SYF2 homolog, RNA splicing factor), also known as hSYF2 or XAB1. is a conserved eukaryotic protein involved in RNA splicing and cell cycle regulation. It was initially identified through its homology to the yeast SYF2. a component of the pre-mRNA splicing machinery. In humans, SYF2 interacts with the XAB2 complex, linking splicing processes to transcription-coupled DNA repair. Structurally, SYF2 contains an N-terminal SYS domain critical for protein-protein interactions and spliceosome assembly.
Functionally, SYF2 participates in multiple steps of spliceosome activation, particularly in recruiting U5 small nuclear ribonucleoprotein (snRNP) during spliceosome maturation. Emerging studies reveal its dual role in genome stability: it facilitates proper splicing of transcripts encoding DNA repair proteins while directly participating in cell cycle checkpoints. Dysregulation of SYF2 has been associated with carcinogenesis, where its overexpression promotes tumor cell proliferation, migration, and chemoresistance.
Recombinant human SYF2 protein is widely used to study spliceosome dynamics, investigate splicing-related diseases, and screen potential anticancer drugs targeting RNA processing. Its recombinant form is typically produced in *E. coli* or mammalian expression systems for structural and functional analyses. Current research focuses on elucidating its moonlighting roles in linking RNA splicing to DNA damage responses, making it a potential therapeutic target for cancers and neurodegenerative disorders.
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