| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SF1 |
| Uniprot No | Q13285 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-461aa |
| 氨基酸序列 | MDYSYDEDLDELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKHYTCTESQSCKIDKTQRKRCPFCRFQKCLTVGMRLEAVRADRMRGGRNKFGPMYKRDRALKQQKKAQIRANGFKLETGPPMGVPPPPPPAPDYVLPPSLHGPEPKGLAAGPPAGPLGDFGAPALPMAVPGAHGPLAGYLYPAFPGRAIKSEYPEPYASPPQPGLPYGYPEPFSGGPNVPELILQLLQLEPDEDQVRARILGCLQEPTKSRPDQPAAFGLLCRMADQTFISIVDWARRCMVFKELEVADQMTLLQNCWSELLVFDHIYRQVQHGKEGSILLVTGQEVELTTVATQAGSLLHSLVLRAQELVLQLLALQLDRQEFVCLKFIILFSLDLKFLNNHILVKDAQEKANAALLDYTLCHYPHCGDKFQQLLLCLVEVRALSMQAKEYLYHKHLGNEMPRNNLLIEMLQAKQT |
| 预测分子量 | 59.1 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3篇与SF1重组蛋白相关的文献示例(内容基于学术领域常见研究方向合理推测，非真实文献)：
1. **文献名称**：*Structural insights into SF1-mediated RNA splicing*
**作者**：Smith J. et al.
**摘要**：通过X射线晶体学解析SF1重组蛋白的RNA结合结构域三维结构，揭示其识别pre-mRNA分支位点的分子机制，阐明SF1在剪接体组装中的关键作用。
2. **文献名称**：*Functional analysis of SF1 in homologous recombination repair*
**作者**：Chen L., Wang H.
**摘要**：利用重组SF1蛋白进行体外生化实验，证明其通过与RAD51等修复蛋白相互作用，促进DNA双链断裂修复过程中的同源重组效率。
3. **文献名称**：*SF1 overexpression enhances cellular transformation in vitro*
**作者**：Garcia R. et al.
**摘要**：研究显示，重组SF1蛋白在癌细胞系中异常高表达可激活MAPK信号通路，促进细胞增殖和迁移，提示其作为癌症治疗潜在靶点的可能性。
注：以上文献为示例性质，实际引用时请通过PubMed或Web of Science检索真实文献。
SF1 (Splicing Factor 1), also known as mammalian branch point-binding protein (mBBP), is a critical component in the pre-mRNA splicing machinery. It plays a pivotal role in recognizing the branch site within introns during the early stages of spliceosome assembly, facilitating the excision of non-coding sequences and ligation of exons. SF1 contains a conserved RNA recognition motif (RRM) and a transiently interacting domain that cooperates with U2AF (U2 snRNP auxiliary factor) to stabilize the commitment complex in splice site selection. Its function is tightly regulated through phosphorylation and interactions with other splicing factors, ensuring precision in alternative splicing events that contribute to transcriptome diversity.
Recombinant SF1 protein is typically produced using heterologous expression systems, such as *E. coli* or insect cells, enabling large-scale purification for structural and functional studies. The recombinant form retains the ability to bind RNA and participate in spliceosome assembly, making it invaluable for *in vitro* splicing assays, crystallography, and mechanistic studies of splicing regulation. Researchers utilize SF1 to investigate diseases linked to splicing errors, including cancers and neurodegenerative disorders, where aberrant splicing contributes to pathogenesis. Additionally, it serves as a tool for screening small molecules targeting spliceosome components for therapeutic development.
Despite its established role in splicing, SF1’s dynamic interactions and regulatory mechanisms remain active areas of research. Studies on recombinant SF1 continue to uncover its context-dependent roles in gene expression, highlighting its potential as a biomarker or therapeutic target in splicing-related diseases.
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