| WB | DB: 1/500 | 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 | Serine/threonine-protein kinase ULK1, Autophagy-related protein 1 homolog, ATG1, hATG1, Unc-51-like kinase 1, ULK1, KIAA0722 |
| Entrez GeneID | 8408 |
| WB Predicted band size | 112.6kDa |
| 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 | This ULK1 Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding S317 of human ULK1. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是3篇涉及Phospho-ULK1(S317)抗体的参考文献，按文献名称、作者及摘要内容简要概括：
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1. **"AMPK Phosphorylates ULK1 to Regulate Autophagy in Response to Energy Stress"**
*作者：Egan et al. (2011)*
**摘要**：研究揭示AMPK通过磷酸化ULK1的S317位点(及其他位点)激活自噬，能量应激条件下(如葡萄糖剥夺)促进自噬体形成，实验中使用Phospho-ULK1(S317)抗体验证位点特异性磷酸化。
2. **"ULK1 Induces Autophagy by Phosphorylating Beclin-1 and Activating VPS34 Lipid Kinase"**
*作者：Russell et al. (2013)*
**摘要**：探讨ULK1在自噬启动中的多重作用，通过Phospho-ULK1(S317)抗体证实mTOR抑制后S317磷酸化水平升高，并阐明该修饰对Beclin-1结合的调控机制。
3. **"Phosphorylation of ULK1 by AMPK Regulates Translocation of ULK1 to Mitochondria and Mitophagy"**
*作者：Toyama et al. (2016)*
**摘要**：发现AMPK介导的ULK1 S317磷酸化驱动线粒体自噬(mitophagy)，研究利用特异性抗体证明该位点磷酸化对ULK1线粒体定位的关键作用。
4. **"Dynamic MTORC1-TFEB Crosstalk in Regulation of ULK1 and Autophagy"**
*作者：Nazio et al. (2019)*
**摘要**：分析mTORC1-TFEB通路对ULK1活性的调控，通过Phospho-ULK1(S317)抗体检测营养充足/缺乏条件下的磷酸化变化，揭示其与自噬-溶酶体系统的关联。
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以上文献均涉及Phospho-ULK1(S317)抗体的应用，重点关注该位点在自噬调控、能量应激响应及疾病机制中的功能。
The Phospho-ULK1 (Ser317) antibody is a critical tool for studying autophagy regulation, specifically targeting the serine 317 phosphorylation site of Unc-51-like kinase 1 (ULK1). ULK1 is a conserved serine/threonine kinase that acts as a master regulator of autophagy initiation. Its activity is tightly controlled by post-translational modifications, particularly phosphorylation events mediated by upstream signaling pathways such as AMP-activated protein kinase (AMPK) and mechanistic target of rapamycin (mTOR). Phosphorylation at Ser317 is associated with ULK1 activation, often occurring under energy-deprived conditions when AMPK is activated. This modification promotes autophagy by enabling ULK1 to phosphorylate downstream substrates involved in autophagosome formation.
Researchers use the Phospho-ULK1(S317) antibody to investigate autophagy dynamics in diverse contexts, including cancer, neurodegeneration, and metabolic disorders. It helps detect ULK1 activation status through techniques like Western blotting, immunofluorescence, or immunoprecipitation. The antibody's specificity for the phosphorylated Ser317 epitope allows differentiation between active and inactive ULK1 forms, providing insights into cellular stress responses. Validation typically includes testing in ULK1-deficient cells or samples treated with phosphatases to confirm phosphorylation dependency. Understanding ULK1 regulation via this antibody has advanced mechanistic studies of autophagy-related diseases and therapeutic interventions targeting this pathway.
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