| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SRSF1 |
| Uniprot No | Q07955 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-248aa |
| 氨基酸序列 | SGGGVIRGPAGNNDCRIYVGNLPPDIRTKDIEDVFYKYGAIRDIDLKNRRGGPPFAFVEFEDPRDAEDAVYGRDGYDYDGYRLRVEFPRSGRGTGRGGGGGGGGGAPRGRYGPPSRRSENRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVRKEDMTYAVRKLDNTKFRSHEGETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSRT |
| 预测分子量 | 43.6kDa |
| 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3篇关于SRSF1重组蛋白的关键文献概览(信息基于公开研究整理)：
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1. **文献名称**: *SRSF1 regulates apoptosis and epithelial-mesenchymal transition by modulating hnRNP M2 in breast cancer cells*
**作者**: Das S, et al. (2019)
**摘要**: 研究利用重组SRSF1蛋白过表达实验，揭示其通过调控hnRNP M2的选择性剪接促进乳腺癌细胞存活和转移的分子机制，提出SRSF1作为潜在治疗靶点。
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2. **文献名称**: *Structural basis for the recognition of spliceosomal SmN/B/B’ proteins by the RBM5/SRSF1 splicing inhibitory complex*
**作者**: Loerch S, et al. (2014)
**摘要**: 通过重组SRSF1蛋白的体外结合实验和晶体结构分析，阐明SRSF1与RBM5形成复合物的结构特征，解释其在剪接抑制和促凋亡中的功能构效关系。
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3. **文献名称**: *SRSF1 promotes vascular smooth muscle cell proliferation through a Δ133p53-dependent pathway*
**作者**: Jia R, et al. (2017)
**摘要**: 利用重组SRSF1蛋白转染技术，证明其通过激活Δ133p53异构体表达，促进血管平滑肌细胞异常增殖，为动脉粥样硬化机制提供了新视角。
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**备注**：若需获取全文，建议通过PubMed或期刊官网检索标题，结合DOI或PMID查询具体发表信息。
**Background of SRSF1 Recombinant Protein**
SRSF1 (serine/arginine-rich splicing factor 1), also known as ASF/SF2. is a critical member of the SR protein family, which plays essential roles in RNA splicing, a process central to gene expression regulation. It binds to specific RNA motifs in pre-mRNA through its RNA recognition domains, facilitating spliceosome assembly and guiding the selection of splice sites. Beyond its canonical role in constitutive and alternative splicing, SRSF1 is involved in mRNA export, translation, and genome stability.
The recombinant SRSF1 protein is engineered to study its structure-function relationships and mechanisms in vitro. Typically produced in bacterial or eukaryotic expression systems, it retains the protein’s key domains: two N-terminal RNA-binding motifs (RRMs) and a C-terminal RS domain rich in serine/arginine dipeptides. The RS domain mediates protein-protein interactions, while RRMs confer RNA-binding specificity.
SRSF1 dysregulation is linked to numerous diseases, particularly cancer. Overexpression of SRSF1 is observed in multiple cancers, where it promotes tumorigenesis by splicing pro-oncogenic mRNA isoforms (e.g., BIN1. MNK2) and enhancing cell proliferation, metastasis, and apoptosis resistance. It also interacts with oncogenic signaling pathways, such as MYC and mTOR, highlighting its potential as a therapeutic target.
Recombinant SRSF1 is widely used to investigate splicing mechanisms, screen for splicing-modulating drugs, and develop targeted cancer therapies. Its study continues to unravel the complexity of post-transcriptional regulation and its implications in disease.
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