Phospho-ACCα (S80)

Cat Number: ABP-0298
Conjugate: Unconjugated
Size: 100 ug
Clone: Poly
Concentration: 1mg/ml
Host: Rb
Isotype: IgG
Immunogen: The antiserum was produced against synthesized peptide derived between 46-95 amino acids from the N-Terminal region of human ACC1 around the phosphorylation site of Ser80.
Reactivity: Hu, Ms, Rt

Western blotting 1:500-1:3000 Immunohistochemistry (Paraffin) 1:150-100 Elisa: 1:1000

Molecular: 280 kDa
Purification: Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser79 of rat ACC. Antibodies are purified by protein A and peptide affinity chromatography.

Acetyl-CoA carboxylase (ACC) catalyzes the pivotal step of the fatty acid synthesis pathway. The 265 kDa ACCis the predominant isoform in liver, adipocytes and mammary gland, while the 280 kDa ACCis the major isoform in skeletal muscle and heart (1). Phosphorylation by AMPK at Ser79, or by PKA at Ser1200, inhibits the enzymatic activity of ACC (2). ACC is a potential target of anti-obesity drugs (3,4).Phospho-Acetyl-CoA Carbox-ylase (Ser79) Antibody detects endogenous levels of ACC only when phosphorylated at serine 79.

Form: liquid
Buffer: Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Storage: Store at –20°C. Do not aliquot the antibody.

Immunohistochemical analysis of paraffin-embedded human breast carcinoma, showing cytoplasmic localization, using Phospho-Acetyl-CoA Carboxylase (Ser79) Antibody.


Immunohistochemical analysis of paraffin-embedded NIH/3T3 cells, untreated (left) or serum-starved (right), using Phospho-Acetyl-CoA Carboxylase (Ser79) Antibody.


Western blot analysis of extracts from K562 cells treated with Insulin 0.01U/ml 15′, using Acetyl CoA Carboxylase (Phospho-Ser80) Antibody. The lane on the right is treated with the synthesized peptide.


(1)Ruderman, N.B. et al. (1999) Am. J. Physiol. 276, E1–E18. (2)Ha, J. et al. (1994) J. Biol. Chem. 269, 22162–22168. (3)Abu-Elheiga, L. et al. (2001) Science 291, 2613–2616. (4)Levert, K.L. et al. (2002) J. Biol. Chem. 277, 16347–16350.