DATASHEET
Host:
Rabbit
Target Protein:
ACACA
Clonality:
Polyclonal
Isotype:
IgG
Source:
KLH conjugated synthetic peptide derived from human ACACA
Purification:
Purified by Protein A.
Storage Buffer:
Aqueous buffered solution containing 0.01M TBS (pH 7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
Storage:
Store at -20°C for 12 months.
Background:
Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. Exercise diminishes the activity of acetyl-CoA carboxylase in human muscle. ACC alpha (ACC1) is the rate-limiting enzyme in the biogenesis of long-chain fatty acids, and ACC∫ (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 ACC alpha 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 enzyme’s short-term regulatory mechanism. The gene encoding ACC alpha maps to human chromosome 17 and encodes a form of ACC, which is the major ACC in lipogenic tissues. The catalytic core of ACC∫ is homologous to that of the ACCå, except for an additional peptide of about 150 amino acids at the N-terminus.