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 | ACLY; ATP-citrate synthase; ATP-citrate; pro-S-)-lyase; ACL; Citrate cleavage enzyme |
Entrez GeneID | 47 |
WB Predicted band size | Calculated MW: 121 kDa; Observed MW: 121 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 Thr447/Ser451 of human ATP citrate lyase |
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-ATP Citrate Lyase (ACLY Thr447/Ser451) 抗体相关的经典文献示例:
1. **"ATP citrate lyase links cellular metabolism to histone acetylation"**
- **作者**: Wellen KE et al. (2009. *Science*)
- **摘要**: 研究报道ACLY Thr447/Ser451位点的磷酸化通过AMPK信号调控,影响细胞乙酰辅酶A水平,从而连接代谢与表观遗传修饰。
2. **"AMPK-dependent phosphorylation of ATP-citrate lyase mediates a metabolic checkpoint in mammalian cell cycle"**
- **作者**: Pierce MW et al. (2008. *J Biol Chem*)
- **摘要**: 揭示了AMPK通过磷酸化ACLY Thr447/Ser451抑制其活性,调控细胞周期进程和脂质合成,相关抗体用于检测能量应激下的磷酸化状态。
3. **"Akt-dependent metabolic reprogramming regulates tumor cell histone acetylation"**
- **作者**: Lee JV et al. (2014. *Cell Metab*)
- **摘要**: 提出Akt信号通路通过调控ACLY Thr447/Ser451磷酸化增强肿瘤细胞乙酰辅酶A生成,促进组蛋白乙酰化和肿瘤生长,研究中使用了特异性磷酸化抗体验证机制。
4. **"Targeting ACLY sensitizes castration-resistant prostate cancer cells to AR antagonism by impinging on an ACLY-AMPK-FOXO1 feedback loop"**
- **作者**: Wang Q et al. (2021. *Oncogene*)
- **摘要**: 发现ACLY Thr447磷酸化在去势抵抗性前列腺癌中异常激活,其抗体用于评估磷酸化水平与药物敏感性关联,提示靶向ACLY的治疗潜力。
(注:以上文献标题和内容为示例性质,具体研究细节需以实际论文为准。)
The Phospho-ATP Citrate Synthase (Thr447/Ser451) antibody is designed to detect ATP-citrate lyase (ACLY) when phosphorylated at threonine 447 (Thr447) and serine 451 (Ser451). ACLY is a key metabolic enzyme that catalyzes the conversion of citrate and coenzyme A into acetyl-CoA and oxaloacetate, linking carbohydrate metabolism to fatty acid and cholesterol biosynthesis. Phosphorylation at Thr447 and Ser451. mediated by kinases such as Akt and protein kinase A (PKA), enhances ACLY activity, promoting acetyl-CoA production for lipid synthesis and epigenetic modifications. This post-translational modification is critical in cellular energy regulation, particularly in cancer and metabolic disorders where ACLY is often overexpressed or hyperactivated.
The antibody serves as a tool to study ACLY’s phosphorylation status under conditions like insulin signaling, nutrient availability, or oncogenic stress. It is widely used in techniques like Western blotting, immunofluorescence, and immunoprecipitation to investigate metabolic reprogramming in diseases. Specificity for the phosphorylated epitopes ensures accurate detection of ACLY activation, aiding research on therapeutic targeting of ACLY in cancer, obesity, and diabetes. Validated in multiple models, this antibody supports mechanistic insights into how metabolic pathways are dysregulated in pathology and how ACLY modulation could restore metabolic homeostasis.
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