For WB: Use at a concentration of 0.5-2ug/ml. Optimal dilutions/concentrations should be determined by the end user.
RIPA lysate from mouse heart cytosol
AcCoA Carboxylase phosphorylated at Ser79
PBS pH7.4 containing 0.05% sodium azide and 30% glycerol
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
1 mg/ml (Please refer to the vial label for the specific concentration.)
Synthetic peptide - amino acids 73–85 of rat Acetyl-CoA Carboxylase 1 [C-HMRSSM[pS]GLHLVK] (KLH)
Protein A affinity purified
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Acetyl-Coa Carboxylase Alpha,Acc1,Acac,Acaca
In cells, excess of metabolic fuel is converted into fatty acids in cytosol and oxidized later in mitochondria to generate ATP and acetyl-CoA. In fatty acid synthesis, catalytic formation of malonyl-CoA (precursor for long-chain fatty acyl-CoA, LCFA-CoA) from acetyl-CoA by Acetyl-CoA carboxylase (ACC-1) is the rate limiting step. The translocation of LCFA-CoA from cytosol to mitochondria is catalyzed by two carnitine palmitoyl transferases (CPT-1 & CPT-2) and regulated by ACC-2, the rate limiting step of mitochondrial fatty acid b-oxidation. Activities of ACC-1 and 2 are regulated by their phosphorylation by 5'-AMP-activated protein kinase (AMPK). Diabetes deranges AMPK master-switch and represses the ACC-1 gene-expression and stimulates excessive fatty acid oxidation which in turn interferes with glucose metabolism. ACC1 is also known as ACC-alpha is a cytosolic enzyme, enriched in liver, adipose and lactating mammary tissues. ACC1 catalyzes the carboxylation of acetyl-CoA to form malonyl-CoA, the rate-limiting step in the biogenesis of LCFA-CoA. ACC1 carries three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase (catalytic activity). Two variants of ACC-1 have been described. One with 8 additional amino acids commencing at Pro-1196. The other which is 59aa shorter than the predominant fat and liver isoform exist in mammals. The presence of 8 additional amino acids inhibits the in vitro phosphorylation of the Ser1200 by camp-dependent kinase. The two ACC1 isoforms are differentially regulated in a tissue specific manner and under different physiological conditions. The activity of ACC1 is finely regulated by hormone dependent phosphorylation and dephosphorylation.