IHC 1:200-1:1000; WB 1:1000-1:15000; IF 1:200-1:1000; ELISA 1:5000-1:20000; IP 1:50-1:200;
Formulation
PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA
Specificity
Acetyl-CoA Carboxylase (Phospho Ser79) Monoclonal Antibody detects endogenous levels of ACC protein only when phosphorylated at S79.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):SSmSG
Purification
Protein A
Storage
-15°C to -25°C/1 year(Do not lower than -25°C)
MW(Calculated)
266kD
MW(Observed)
266kD
Modification
Phospho
Clonality
Monoclonal
Clone Number
PT0983R
Isotype
IgG, Kappa
Related Products
Secondary Antibodies
Goat Anti Mouse IgG(H+L) (HRP)
RS0001
More→
Secondary Antibodies
Goat Anti Rabbit IgG(H+L) (HRP)
RS0002
More→
Primary Antibodies
β-actin (PTR2364) Mouse mAb
YM3028
More→
Primary Antibodies
GAPDH (PTR2304) Mouse mAb
YM3029
More→
Antigen&Target Information
Specificity:
Acetyl-CoA Carboxylase (Phospho Ser79) Monoclonal Antibody detects endogenous levels of ACC protein only when phosphorylated at S79.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):SSmSG
Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. ACC-beta is thought to control fatty acid oxidation by means of the ability of malonyl-CoA to inhibit carnitine-palmitoyl-CoA transferase I, the rate-limiting step in fatty acid uptake and oxidation by mitochondria. ACC-beta may be involved in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. There is evidence for the presence of two ACC-beta isoforms. [provided by RefSeq, Jul 2008],
show all
Function:
Catalytic activity:ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA.,Catalytic activity:ATP + biotin-carboxyl-carrier protein + CO(2) = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.,cofactor:Binds 2 manganese ions per subunit.,cofactor:Biotin.,enzyme regulation:Activated by citrate. Inhibited by malonyl-CoA.,Function:ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.,pathway:Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.,similarity:Contains 1 ATP-grasp domain.,similarity:Contains 1 biotin carboxylation domain.,similarity:Contains 1 biotinyl-binding domain.,similarity:Contains 1 carboxyltransferase domain.,subcellular location:May associate with membranes.,tissue specificity:Predominantly expressed in the heart, skeletal muscles and liver.,
show all
Cellular Localization:
Mitochondrion
show all
Tissue Expression:
Widely expressed with highest levels in heart, skeletal muscle, liver, adipose tissue, mammary gland, adrenal gland and colon (PubMed:9099716). Isoform 3 is expressed in skeletal muscle, adipose tissue and liver (at protein level) (PubMed:19190759). Isoform 3 is detected at high levels in adipose tissue with lower levels in heart, liver, skeletal muscle and testis (PubMed:19190759).