Product Pathways - Metabolism
Phospho-Acetyl-CoA Carboxylase (Ser79) Antibody #3661
|W IP IHC-P||H M R Mk (C) (B)||Endogenous||280||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey C=Chicken B=Bovine
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Phospho-Acetyl-CoA Carboxylase (Ser79) Antibody detects endogenous levels of ACC only when phosphorylated at serine 79. The antibody recognizes both ACCalpha and ACCbeta.
Source / 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.
Western blot analysis of extracts from HEK293 cells, untreated or oligomycin-treated, using Phospho-Acetyl-CoA Carboxylase (Ser79) 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.
Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to malonyl-CoA (1). It is the key enzyme in the biosynthesis and oxidation of fatty acids (1). In rodents, the 265 kDa ACC1 (ACCα) form is primarily expressed in lipogenic tissues, while 280 kDa ACC2 (ACCβ) is the main isoform in oxidative tissues (1,2). However, in humans, ACC2 is the predominant isoform in both lipogenic and oxidative tissues (1,2). Phosphorylation by AMPK at Ser79 or by PKA at Ser1200 inhibits the enzymatic activity of ACC (3). ACC is a potential target of anti-obesity drugs (4,5).
- Castle, J.C. et al. (2009) PLoS One 4, e4369.
- Kreuz, S. et al. (2009) Diabetes Metab Res Rev 25, 577-86.
- Ha, J. et al. (1994) J Biol Chem 269, 22162-8.
- Abu-Elheiga, L. et al. (2001) Science 291, 2613-6.
- Levert, K.L. et al. (2002) J Biol Chem 277, 16347-50.
- Hadad, S.M. et al. (2009) BMC Cancer 9, 307.
- Morales-Alamo, D. et al. (2013) J Appl Physiol 114, 566-77. Applications: Western Blotting
- Morales-Alamo, D. et al. (2012) J Appl Physiol 113, 917-28. Applications: Western Blotting
- Mihaylova, M.M. et al. (2011) Cell 145, 607-21. Applications: Western Blotting
- Kumazawa, T. et al. (2011) J Biol Chem 286, 20861-9. Applications: Western Blotting
- Vigetti, D. et al. (2011) J Biol Chem 286, 7917-24. Applications: Western Blotting
- Göransson, O. et al. (2007) J Biol Chem 282, 32549-60. Applications: Western Blotting
- Aymerich, I. et al. (2006) J Cell Sci 119, 1612-21. Applications: Western Blotting
- Shaw, R. J. et al. (2004) The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress. PNAS 101 (10), 3329-3335. Applications: Western Blotting
- Pilon, G. et al. (2004) Inhibition of Inducible Nitric-oxide Synthase by Activators of AMP-activated Protein Kinase. The Journal of Biological Chemistry 279 (20), 20767-20774. Applications: Western Blotting
- Gonzalez, A.A. et al. (2004) Am J Physiol Endocrinol Metab 287, E1032-7. Applications: Western Blotting
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For Research Use Only. Not For Use In Diagnostic Procedures.