ACC-1 - Detailed product view

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Article Nr AAD-44957
Description Anti-Human Acetyl-CoA Carboxylase-1 (ACC1) , polyclonal
Sizes 100 ┬Ál
Format serum
Source/Host rabbit
Immunogen r/h, 15 aa ~NT
Clone polyclonal
Applications ELISA, WB
Species Reactivity human, mouse, rat, cow/bovine
Protocol   Western Blotting (1:1K-5K for neat serum and 1-10 ug/ml for affinity pure using Chemiluminescence technique).ELISA (1:10K-1:100K; using 50-100 ng of control peptide/well).
References   : (1) Munday MR et al (1988) Eur. J. Biochem. 175, 331; Abu-Elheiga et al. (2000) PNAS 97, 1444; Lee et al. (2001) J. Biol. Chem 276, 2576; Abu-Elheiga et al. (1997) J. Biol. Chem. 272, 10699; Hoppel et al. (2001) ABB 392, 321; Fraser & Zammit (1998) Biochem. J. 329, 225.Stapleton et al. (1996) J. Biol. Chem. 271, 611; Mitchelhill et al. (1997) J. Biol. Chem. 272, 24475
Notes   ACC1 (rat 2345-aa, human 2345-aa, ~265 kDa, chromosome 17q21) is also known as ACC-alpha is a cytosolic enzyme, enriched in liver, adipose and lactating mammary tissues. ACC-1 from rat, human, chicken are over 90% identical. 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, and the other which is 59 aa 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 isoform 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
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