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     Western blot analysis of HSP90B expression in (1)HepG2 cell lysate; (2)SH-SY5Y cell lysate.    

  
  

Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, a critical rate-limiting step in fatty acid synthesis and regulation. It exists in two isoforms: ACC1 (cytosolic) and ACC2 (mitochondrial), which regulate lipid synthesis and oxidation, respectively. Dysregulation of ACC activity is linked to metabolic disorders (e.g., obesity, diabetes) and cancers, making it a therapeutic target.

ACC antibodies are immunodetection tools used to study ACC expression, phosphorylation, and subcellular localization in metabolic research. In clinical contexts, autoantibodies targeting ACC (anti-ACC antibodies) are associated with autoimmune hepatitis (AIH), particularly type 1 AIH. These autoantibodies, often detected via immunoassays, are part of the diagnostic workup alongside other markers (e.g., anti-SLA/LP antibodies). Their presence correlates with disease activity and may inform prognosis.

Research-grade ACC antibodies (monoclonal/polyclonal) are widely utilized in Western blotting, immunohistochemistry, and functional inhibition studies to explore ACC's role in cellular metabolism and disease mechanisms. Recent drug development efforts targeting ACC for metabolic syndrome or cancer therapy have further driven the demand for specific, high-affinity ACC antibodies to assess target engagement and therapeutic efficacy.