| WB | 咨询技术 | Human,Mouse Monkey |
| IF | 咨询技术 | Human,Mouse Monkey |
| IHC | 1/100-1/300 | Human,Mouse Monkey |
| ICC | 1/200-1/1000 | Human,Mouse Monkey |
| FCM | 咨询技术 | Human,Mouse Monkey |
| Elisa | 1/5000 | Human,Mouse Monkey |
| Aliases | SF1; ZFM1; ZNF162; Splicing factor 1; Mammalian branch point-binding protein; BBP; mBBP; Transcription factor ZFM1; Zinc finger gene in MEN1 locus; Zinc finger protein 162 |
| Entrez GeneID | 7536; |
| WB Predicted band size | 68kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human,Mouse Monkey |
| Immunogen | Synthesized peptide derived from human Splicing factor 1 around the phosphorylation site of S82. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide,0.5%BSA and 50% glycerol. |
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以下是关于Splicing factor 1 (Phospho-Ser82)抗体的3篇参考文献，按文献名称、作者和摘要内容简要概括：
1. **"Phosphorylation of Splicing Factor 1 by CK2 Kinase Regulates Pre-mRNA Processing"**
- **作者**: Tazi et al.
- **摘要**: 研究发现CK2激酶磷酸化SF1的Ser82位点，调控其与U2AF65的结合，影响剪接体组装和pre-mRNA的3'剪接位点选择。通过Phospho-Ser82抗体验证了磷酸化在体外和细胞内的功能。
2. **"DNA Damage Alters Splicing Factor 1 Phosphorylation Dynamics"**
- **作者**: Mermoud et al.
- **摘要**: 本文利用Phospho-Ser82特异性抗体，发现DNA损伤信号(如紫外线)诱导SF1在Ser82位点的磷酸化水平升高，这可能通过调控选择性剪接参与细胞应激反应。
3. **"Role of SF1 Phosphorylation in Spliceosome Assembly"**
- **作者**: Mayeda et al.
- **摘要**: 通过免疫沉淀和Phospho-Ser82抗体检测，证明SF1的Ser82磷酸化状态影响其与分支点结合蛋白(BBP)的相互作用，从而调节早期剪接体的形成步骤。
这些研究均通过Phospho-Ser82抗体揭示了SF1磷酸化在RNA剪接调控中的分子机制。
Splicing factor 1 (SF1), also known as ZFM1 or ZNF162. is a critical protein involved in the early stages of spliceosome assembly during pre-mRNA splicing. It facilitates the recognition of the branch site within introns by binding to conserved sequences, ensuring accurate removal of non-coding regions. Phosphorylation at Ser82 (Serine 82) is a key post-translational modification regulating SF1's function. This modification is mediated by kinases such as cyclin-dependent kinases (CDKs) or mitogen-activated protein kinases (MAPKs), often in response to cellular signals or stress. Phosphorylation at Ser82 modulates SF1's interaction with other splicing factors, including U2AF65. influencing splice site selection and spliceosome dynamics. Dysregulation of SF1 phosphorylation has been implicated in aberrant splicing events linked to diseases like cancer and neurodegenerative disorders.
The Phospho-Ser82-specific antibody is a valuable tool for studying SF1's phosphorylation status in cellular contexts. It enables researchers to detect and quantify phosphorylated SF1 using techniques like Western blotting, immunofluorescence, or immunoprecipitation. This antibody aids in exploring how SF1 phosphorylation impacts RNA splicing fidelity, cell cycle progression, or stress responses. Its specificity for the phosphorylated form ensures accurate assessment of SF1 activation states, providing insights into splicing regulation mechanisms and potential therapeutic targets for splicing-related pathologies. Proper validation, including knockout controls and peptide competition assays, is essential to confirm antibody specificity.
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