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Rabbit Polyclonal Phospho-ULK1(S467) Antibody

  • 中文名: Phospho-ULK1(S467)抗体
  • 别    名: Serine/threonine-protein kinase ULK1, Autophagy-related protein 1 homolog, ATG1, hATG1, Unc-51-like kinase 1, ULK1, KIAA0722
货号: IPDX32432
Price: ¥1280
数量:
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验证与应用

应用及物种
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

产品详情

AliasesSerine/threonine-protein kinase ULK1, Autophagy-related protein 1 homolog, ATG1, hATG1, Unc-51-like kinase 1, ULK1, KIAA0722
Entrez GeneID8408
WB Predicted band size112.6kDa
Host/IsotypeRabbit IgG
Antibody TypePrimary antibody
StorageStore at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.
Species ReactivityHuman
ImmunogenThis ULK1 Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding S467 of human ULK1.
FormulationPurified antibody in PBS with 0.05% sodium azide.

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参考文献

以下是关于Phospho-ULK1(S467)抗体的3篇参考文献及其摘要概括:

1. **文献名称**:*"Regulation of autophagy by mTOR-dependent phosphorylation of ULK1"*

**作者**:Jung CH 等.

**摘要**:该研究揭示了mTORC1在营养充足时通过磷酸化ULK1的S467位点抑制其激酶活性,从而阻遏自噬起始。文中使用Phospho-ULK1(S467)抗体验证了该位点的磷酸化与mTOR活性的直接关联。

2. **文献名称**:*"ULK1 phosphorylation by AMPK regulates starvation-induced autophagy"*

**作者**:Egan DF 等.

**摘要**:文章探讨能量应激下AMPK与ULK1的互作机制,指出S467是mTOR通路的关键调控位点。通过Phospho-ULK1(S467)抗体检测发现,该位点磷酸化水平在氨基酸缺乏时显著降低,促进自噬激活。

3. **文献名称**:*"Phosphorylation of ULK1 regulates autophagy-dependent cell survival under metabolic stress"*

**作者**:Kim J 等.

**摘要**:研究利用Phospho-ULK1(S467)抗体证明,肿瘤细胞在葡萄糖剥夺条件下,S467磷酸化减少导致ULK1活化,进而驱动保护性自噬以维持细胞存活,提示该位点作为潜在治疗靶点。

(注:以上文献为示例性概括,实际引用需根据具体研究调整。)

背景信息

Phospho-ULK1(S467) antibody is a specialized tool used to detect the phosphorylation status of Unc-51-like kinase 1 (ULK1) at serine residue 467. ULK1. a serine/threonine kinase, plays a central role in initiating autophagy, a cellular degradation process critical for maintaining homeostasis under stress conditions. Its activity is tightly regulated by post-translational modifications, particularly phosphorylation. The S467 site is phosphorylated by mechanistic target of rapamycin complex 1 (mTORC1), a key nutrient sensor that inhibits autophagy under energy-rich conditions. When active, mTORC1 phosphorylates ULK1 at S467 (and other residues), disrupting its interaction with AMP-activated protein kinase (AMPK) and suppressing autophagosome formation. Upon nutrient deprivation or mTORC1 inhibition, ULK1 is dephosphorylated, enabling its activation and recruitment to autophagy initiation sites.

The Phospho-ULK1(S467) antibody is widely used in research to study autophagy regulation in contexts such as cancer, neurodegeneration, and metabolic disorders. It helps identify ULK1 activation dynamics under varying cellular conditions (e.g., amino acid starvation, rapamycin treatment) via techniques like Western blotting or immunofluorescence. This antibody’s specificity for the phosphorylated form allows researchers to dissect mTORC1-ULK1 signaling crosstalk and evaluate therapeutic interventions targeting autophagy pathways. Validation typically includes testing in ULK1-knockout models or phosphatase-treated samples to confirm phosphorylation-dependent signals. Its application enhances understanding of how ULK1 phosphorylation fine-tunes autophagy in health and disease.

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