| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 咨询技术 | Human,Mouse,Rat |
| ICC | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | C23; Nsr1 |
| Entrez GeneID | 4691 |
| WB Predicted band size | Calculated MW: 77 kDa; Observed MW: 100 kDa |
| 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 |
| Immunogen | A synthetic phosphopeptide corresponding to residues surrounding Thr84 of human Nucleolin |
| Formulation | Purified antibody in TBS with 0.05% sodium azide,0.05%BSA and 50% glycerol. |
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以下是3篇与Phospho-Nucleolin (Thr84)抗体相关的文献摘要(部分为模拟示例，具体文献可能需要根据实际数据库检索验证)：
1. **文献名称**: *"ATM-dependent phosphorylation of Nucleolin at Thr84 promotes its interaction with MDC1 in DNA damage response"*
**作者**: Sato, Y. et al.
**摘要**: 研究揭示了DNA双链断裂后，ATM激酶磷酸化Nucleolin的Thr84位点，促进其与MDC1蛋白结合，从而调控DNA损伤修复信号的传递。
2. **文献名称**: *"Phosphorylation of Nucleolin on Thr84 regulates its ribosome biogenesis function"*
**作者**: Ghisolfi-Nieto, L. et al.
**摘要**: 报道了Thr84磷酸化通过影响Nucleolin的RNA结合能力，调控核仁内rRNA加工和核糖体组装，与细胞增殖密切相关。
3. **文献名称**: *"Phospho-Nucleolin (Thr84) as a biomarker for Akt/mTOR signaling activity in breast cancer cells"*
**作者**: Ko, H.R., & Meng, Z.X.
**摘要**: 发现乳腺癌中Akt/mTOR通路通过磷酸化Nucleolin Thr84位点增强其稳定性，促进肿瘤细胞存活和侵袭，提示该位点可作为治疗靶点。
4. **文献名称**: *"Dynamic phosphorylation of Nucleolin at Thr84 during cell cycle progression"*
**作者**: Daniely, Y., & Borer, P.N.
**摘要**: 研究表明Thr84磷酸化水平在G1/S期显著升高，可能通过调控Nucleolin的核质穿梭影响细胞周期进程。
**注意**：以上文献为示例性内容，实际引用需通过PubMed或SciFinder等平台检索真实文献(如未找到直接匹配，可扩大关键词至“Nucleolin phosphorylation”或联系抗体供应商获取引用文献)。
**Background of Phospho-Nucleolin (Thr84) Antibody**
Nucleolin is a multifunctional nucleolar protein involved in ribosomal RNA (rRNA) processing, ribosome assembly, and chromatin organization. It also plays roles in cell proliferation, apoptosis, and stress responses. Post-translational modifications, including phosphorylation, regulate its activity and localization. Phosphorylation at Thr84 is implicated in modulating nucleolin’s interactions with other proteins and nucleic acids, particularly during cell cycle progression or stress conditions.
The Phospho-Nucleolin (Thr84) antibody specifically detects nucleolin when phosphorylated at threonine 84. serving as a critical tool for studying its functional regulation. This modification is associated with nucleolin’s redistribution from the nucleolus to the nucleoplasm or cytoplasm under certain stimuli, such as DNA damage or viral infection. Researchers employ this antibody in techniques like Western blotting, immunofluorescence, or immunoprecipitation to explore nucleolin’s role in cancer, viral replication, or cellular stress pathways.
Dysregulation of nucleolin phosphorylation is linked to tumorigenesis and neurodegenerative diseases, making this antibody valuable for both basic research and translational studies. Validating its specificity via knockout/knockdown controls or phosphatase treatment is essential to ensure accurate detection of this dynamic modification.
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