Fatty Acid and Lipid Metabolism Antibody Sampler Kit #8335
Product Information
Kit Usage Information
Protocols
- 3180: Western Blotting, Immunoprecipitation (Agarose), Immunohistochemistry (Paraffin), Immunofluorescence
- 3658: Western Blotting, Immunoprecipitation (Agarose)
- 3676: Western Blotting, Immunoprecipitation (Agarose), Immunohistochemistry (Paraffin), Immunofluorescence, Flow
- 4331: Western Blotting, Immunoprecipitation (Magnetic)
- 4332: Western Blotting
- 7074: Western Blotting
- 9189: Western Blotting, Immunoprecipitation (Agarose)
- 11818: Western Blotting, Immunoprecipitation (Agarose), Immunohistochemistry (Paraffin), Immunofluorescence
- 14906: Western Blotting, Immunoprecipitation (Agarose), Immunofluorescence
Product Description
Specificity / Sensitivity
AceCS1 (D19C6) Rabbit mAb recognizes endogenous levels of total cytoplasmic acetyl-CoA synthetase. Phospho-Acetyl-CoA Carboxylase (Ser79) (D7D11) Rabbit mAb recognizes endogenous levels of ACC only when phosphorylated at Ser79; this antibody recognizes both ACCα and ACCß. Acetyl-CoA Carboxylase (C83B10) Rabbit mAb recognizes endogenous levels of all isoforms of acetyl-CoA carboxylase protein. Phospho-ATP-Citrate Lyase (Ser455) Antibody recognizes endogenous levels of ATP-citrate lyase only when phosphorylated at Ser455. ACSL1 (D2H5) Rabbit mAb, ATP-Citrate Lyase Antibody, Fatty Acid Synthase (C20G5) Rabbit mAb, and Lipin 1 (D2W9G) Rabbit mAb recognize endogenous levels of their respective target proteins.
Source / Purification
Monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the sequence of human cytoplasmic acetyl-CoA synthetase, residues surrounding Ser523 of human acetyl-CoA carboxylase α1, residues surrounding Gly46 of human fatty acid synthase, residues near the carboxy terminus of human lipin 1 or residues surrounding Ala257 of human ACSL1 protein. Monoclonal activation state antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser79 of human acetyl-CoA carboxylase protein. Modification state-specific polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser455 of human ATP-citrate lyase protein. Polyclonal antibodies are produced by immunizing animals corresponding to residues of human ATP-citrate lyase protein. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.
Background
The processes of fatty acid and lipid metabolism are vital for cellular nutrient and energy maintenance. Cytoplasmic acetyl-CoA synthetase (AceCS1) catalyzes the conversion of acetate and CoA to acetyl-CoA. Acetyl-CoA synthesized by AceCS1 is used for fatty acid and lipid biosynthesis (1,2). Acetyl-CoA carboxylase (ACC) catalyzes the pivotal step of the fatty acid synthesis pathway. Phosphorylation by AMPK at Ser79 or by PKA at Ser1200 inhibits the enzymatic activity of ACC (3). Mammalian long-chain acyl-CoA synthetase (ACSL) catalyzes the ligation of the fatty acid to CoA to form fatty acyl-CoA in a two-step reaction (4). ATP-citrate lyase (ACL) is a homotetramer that catalyzes the formation of acetyl-CoA and oxaloacetate (OAA) in the cytosol, which is the key step for the biosynthesis of fatty acids, cholesterol, and acetylcholine, as well as for glucogenesis (5). Phosphorylation of ACL at Ser455 abolishes the homotropic allosteric regulation by citrate and enhances the catalytic activity of the enzyme (6). Fatty acid synthase (FASN) catalyzes the synthesis of long-chain fatty acids from acetyl-CoA and malonyl-CoA (7). Lipin 1 plays a role in lipid metabolism in various tissues and cell types including liver, muscle, adipose tissues, and neuronal cell lines (8-10). It has dual functions at the molecular level: Lipin 1 serves as a transcriptional coactivator in the liver and a phosphatidate phosphatase in triglyceride and phospholipid biosynthesis pathways (11).
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- Luong, A. et al. (2000) J Biol Chem 275, 26458-66.
- Ha, J. et al. (1994) J Biol Chem 269, 22162-8.
- Mashek, D.G. et al. (2004) J Lipid Res 45, 1958-61.
- Towle, H.C. et al. (1997) Annu Rev Nutr 17, 405-33.
- Potapova, I.A. et al. (2000) Biochemistry 39, 1169-79.
- Katsurada, A. et al. (1990) Eur J Biochem 190, 427-33.
- Finck, B.N. et al. (2006) Cell Metab 4, 199-210.
- Phan, J. and Reue, K. (2005) Cell Metab 1, 73-83.
- Verheijen, M.H. et al. (2003) Genes Dev 17, 2450-64.
- Reue, K. and Zhang, P. (2008) FEBS Lett 582, 90-6.
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