磷酸化-乙酰辅酶A羧化酶 (Ser79) 重组兔单克隆抗体 (S-4302)-S0B6884

Phospho-Acetyl-CoA Carboxylase (Ser79) refers to the specific phosphorylated state of Acetyl-CoA Carboxylase 1 (ACC1) at serine residue 79, a critical post-translational modification that serves as a key regulatory switch in lipid metabolism. This phosphorylation is primarily catalyzed by AMP-activated protein kinase (AMPK) in response to cellular energy stress or low ATP levels, leading to the allosteric inhibition of ACC enzymatic activity. By inhibiting ACC, the conversion of acetyl-CoA to malonyl-CoA is blocked, which subsequently reduces de novo fatty acid synthesis and relieves the inhibition of carnitine palmitoyltransferase 1 (CPT1), thereby promoting mitochondrial fatty acid oxidation. Consequently, the detection of ACC phosphorylated at Ser79 is widely used as a biomarker for AMPK activation and the metabolic shift from anabolic lipid storage to catabolic energy production, playing a significant role in the physiological responses to exercise, fasting, and pharmacological interventions targeting metabolic disorders.