Rabbit Monoclonal Phospho-ULK1(S556) Antibody

The Phospho-ULK1 (Ser556) antibody is a key tool for studying autophagy regulation, specifically targeting the phosphorylation status of ULK1 (Unc-51-like kinase 1) at serine residue 556. ULK1 is a central kinase in autophagy initiation, integrating signals from upstream regulators like AMP-activated protein kinase (AMPK) and mechanistic target of rapamycin (mTOR). Phosphorylation at Ser556. mediated by AMPK under energy-deprived conditions, activates ULK1. promoting autophagosome formation and cellular stress adaptation. Conversely, mTOR-dependent signaling under nutrient-rich conditions inhibits ULK1 by phosphorylating distinct residues. This antibody enables researchers to detect ULK1 activation status, distinguishing between active (AMPK-phosphorylated) and inactive (mTOR-inhibited) forms. It is widely used in techniques such as Western blotting and immunofluorescence to investigate autophagy dynamics in response to metabolic stressors, drug treatments, or disease models like cancer, neurodegeneration, or metabolic disorders. Its specificity for the phosphorylated Ser556 epitope makes it critical for elucidating AMPK-ULK1 signaling crosstalk and autophagy-related therapeutic mechanisms. Validation typically includes testing in ULK1-knockout cells or phosphorylation-deficient mutants to confirm specificity. Proper application requires attention to cell treatment conditions (e.g., starvation, AMPK/mTOR modulators) to induce detectable phosphorylation changes.