Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the ratelimiting step in fatty acid synthesis. Exercise diminishes the activity of acetyl- CoA carboxylase in human muscle. ACCalpha (ACC1) is the rate-limiting enzyme in the biogenesis of long-chain fatty acids, and ACCbeta (ACC2) may control mitochondrial fatty acid oxidation. These two isoforms of ACC control the amount of fatty acids in the cells. The catalytic function of ACCalpha is regulated by phosphorylation (inactive) and dephosphorylation (active) of targeted Serine residues and by allosteric transformation by citrate or palmitoyl-CoA, which serve as the short-term regulatory mechanism of the enzyme. The gene encoding ACCalpha, which maps to human chromosome 17, encodes the 265 kDa alpha form of ACC, which is the major ACC in lipogenic tissues. The catalytic core of ACCbeta is homologous to that of ACCalpha except for an additional peptide of about 150 amino acids at the N-terminus.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000 IHC: 1:50~1:200
Application Notes:
p-ACCalpha (S80) polyclonal antibody etects endogenous levels of ACCalpha protein only when phosphorylated at Ser80.
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