| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SRSF2 |
| Uniprot No | Q01130 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-221aa |
| 氨基酸序列 | MSYGRPPPDVEGMTSLKVDNLTYRTSPDTLRRVFEKYGRVGDVYIPRDRYTKESRGFAFVRFHDKRDAEDAMDAMDGAVLDGRELRVQMARYGRPPDSHHSRRGPPPRRYGGGGYGRRSRSPRRRRRSRSRSRSRSRSRSRSRYSRSKSRSRTRSRSRSTSKSRSARRSKSKSSSVSRSRSRSRSRSRSRSPPPVSKRESKSRSRSKSPPKSPEEEGAVSS |
| 预测分子量 | 25,4 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SRSF2重组蛋白的3篇模拟参考文献及其摘要概括(注：文献为示例性虚构，实际需根据真实数据库检索)：
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1. **文献名称**：*Structural Insights into SRSF2 Recombinant Protein in RNA Splicing Regulation*
**作者**：Zhang, Y. et al. (2021)
**摘要**：本研究通过重组表达纯化人源SRSF2蛋白，结合X射线晶体学解析其三维结构，揭示了其RNA结合域(RRM)与靶RNA的相互作用机制，为理解其在剪接体组装中的关键作用提供结构基础。
2. **文献名称**：*SRSF2 Recombinant Mutants Dysregulate Splicing in Myelodysplastic Syndromes*
**作者**：Kim, J.H. et al. (2019)
**摘要**：通过构建携带P95H突变的SRSF2重组蛋白，发现其异常结合特定mRNA前体，导致剪接错误并激活DNA损伤通路，揭示了该突变在骨髓增生异常综合征中的致病机理。
3. **文献名称**：*In Vitro Functional Analysis of SRSF2 Recombinant Protein Using Splicing Reporters*
**作者**：Chen, L. et al. (2020)
**摘要**：利用重组SRSF2蛋白与荧光素酶报告系统，证明其通过调控外显子跳跃影响癌症相关基因(如BCL2L1)的可变剪接，为靶向剪接因子的药物筛选提供实验模型。
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如需真实文献，建议在PubMed或Web of Science中检索关键词“SRSF2 recombinant protein”或“SRSF2 purification”，并筛选近年的功能/结构研究。
**Background of SRSF2 Recombinant Protein**
SRSF2 (serine/arginine-rich splicing factor 2) is a key member of the SR protein family, which plays a critical role in pre-mRNA splicing, a process essential for generating mature mRNA transcripts. As a splicing factor, SRSF2 contains characteristic arginine/serine-rich (RS) domains and RNA recognition motifs (RRMs), enabling it to bind specific RNA sequences and recruit core spliceosome components to regulate splice site selection. This protein is vital for maintaining splicing fidelity, influencing diverse cellular processes, including cell cycle progression, differentiation, and apoptosis.
Recombinant SRSF2 protein is produced using expression systems like *E. coli* or mammalian cells, allowing researchers to study its biochemical properties and interactions in vitro. Purified recombinant SRSF2 retains RNA-binding activity and splicing regulatory functions, making it a valuable tool for dissecting mechanisms of alternative splicing and spliceosome assembly. Studies using this protein have revealed its role in recognizing exonic splicing enhancers (ESEs) and modulating spliceosome dynamics through phosphorylation-dependent interactions.
Dysregulation of SRSF2 is linked to human diseases. Recurrent mutations in SRSF2. particularly proline substitutions at residue P95. are observed in myelodysplastic syndromes (MDS) and acute myeloid leukemia (AML). These mutations alter splicing patterns, leading to aberrant isoform expression of genes involved in epigenetics, signaling, and genome stability. Recombinant mutant SRSF2 proteins have been instrumental in identifying pathogenic splicing errors and evaluating their contribution to oncogenesis.
Furthermore, recombinant SRSF2 is used in drug screening to target spliceosomal vulnerabilities in cancers. Its structural and functional characterization continues to advance therapeutic strategies, such as modulating splicing activity or correcting dysregulated pathways in malignancies. Overall, SRSF2 recombinant protein serves as a cornerstone for understanding RNA splicing mechanisms and their implications in disease.
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