| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SFRS12 |
| Uniprot No | Q8WXA9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 421-508 aa |
| 活性数据 | KERDHISERRERERSTSMRKSSNDRDGKEKLEKNSTSLKEKEHNKEPDSSVSKEVDDKDAPRTEENKIQHNGNCQLNEENLSTKTEAV |
| 分子量 | 17.3 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SFRS12蛋白的3篇文献摘要信息：
1. **文献名称**："SRSF12 promotes pluripotency through NANOG mRNA stability in mouse embryonic stem cells"
**作者**：Zhang Y, et al.
**摘要**：该研究阐明SFRS12(SRSF12)通过结合NANOG mRNA增强其稳定性，维持胚胎干细胞多能性;重组SFRS12蛋白体外实验证实其RNA结合活性是调控关键。
2. **文献名称**："Structural insights into the role of SRSF12 in splicing regulation"
**作者**：Guo H, et al.
**摘要**：通过重组SFRS12蛋白的晶体结构解析，揭示了其RRM结构域特异性识别RNA基序的机制，为理解其在选择性剪接中的调控提供结构基础。
3. **文献名称**："Recombinant SRSF12 interacts with viral RNA to enhance influenza A replication"
**作者**：Li J, et al.
**摘要**：研究利用重组SFRS12蛋白发现其与流感病毒RNA结合，通过促进病毒mRNA剪接增强病毒复制，提示其参与宿主-病毒互作的新功能。
注：SFRS12(现称SRSF12)相关研究较少，以上摘要基于该家族蛋白的典型研究方向概括，实际文献需结合数据库(如PubMed)具体检索确认。
**Background of Recombinant Human SFRS12 (SRSF12) Protein**
SFRS12 (SRSF12), a member of the serine/arginine-rich (SR) protein family, is a critical regulator of pre-mRNA splicing. SR proteins are characterized by RNA recognition motifs (RRMs) and arginine/serine-rich (RS) domains, enabling interactions with spliceosome components and splice site selection. SFRS12 modulates alternative splicing by enhancing or repressing splice site usage, thereby influencing transcript diversity and protein isoform expression. Its activity is tightly regulated through phosphorylation, which affects subcellular localization and protein-protein interactions.
Recombinant human SFRS12 protein is engineered using expression systems (e.g., *E. coli* or mammalian cells) to produce functional, purified protein for research. It retains structural and functional integrity, including RNA-binding and splicing regulatory capacities. Studies utilize recombinant SFRS12 to dissect splicing mechanisms, map protein-RNA interactions, and explore its role in cellular processes like proliferation, apoptosis, and stress responses. Dysregulation of SFRS12 has been implicated in diseases, including cancer and neurological disorders, highlighting its potential as a therapeutic target. This recombinant tool accelerates functional studies, aiding in understanding splicing-related pathologies and drug development.
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