Acetyl-CoA Carboxylase alpha (ACACA) (pSer79) antibody

Details for Product No. ABIN649247
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Antigen
Synonyms AT-ACC1, EMB22, EMBRYO DEFECTIVE 22, GK, GURKE, PAS3, PASTICCINO 3, acetyl-CoA carboxylase 1, ACAC, ACACAD, ACC, ACC1, ACCA, Acac, A530025K05Rik, Acc1, Gm738
Epitope
pSer79
(27), (20), (17), (14), (12), (8), (7), (3), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Human
(116), (67), (62), (24), (24), (24), (12), (12), (12), (1)
Host
Rabbit
(114), (7)
Clonality
Monoclonal
Conjugate
Un-conjugated
(5), (5), (5), (4), (4), (4), (4), (4), (4), (4), (4), (1), (1), (1)
Application
Western Blotting (WB)
(80), (43), (40), (35), (19), (6), (3), (2), (2), (1), (1), (1)
Pubmed 3 references available
Quantity 100 μL
Options
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Catalog No. ABIN649247
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Specificity A phospho specific peptide corresponding to residues surrounding serine 79 of human ACC1 was used as an immunogen. This antibody detects ACC1 phosphorylated at serine 79.
Alternative Name Acetyl-CoA1 (ACC1)
Background Acetyl-CoA carboxylase 1 (ACC1) is a biotin dependent lipogenic enzyme that is highly expressed during adipogenesis. ACC1 catalyzes acetyl-CoA carboxylation, producing malonyl-CoA, a metabolite involved in energy homeostasis regulation. Malonyl-CoA is a two carbon donor in the synthesis of long-chain fatty acids and the elongation of fatty acids found in the cystol (1). ACC1 is regulated short-term by citrate, CoA, and palmitoyl-CoA through allosteric interactions. Nutrients and hormones can be both short-term (inducing reversible phosphorylations by such as AMPK at Ser79 and others) and long-term (transcription level regulation) regulators of ACC1 (2). Highly expressed in lipogenic tissues, ACC1 is found in liver, adipose, and lactating mammary gland (3). ACC1 has been implicated as a target in the development of anti-obesity drugs (4).
Synonyms: ACACA, ACAC, ACC1, ACCA, Biotin carboxylase, ACC-alpha
Molecular Weight 280 kDA
Gene ID 31
UniProt Q13085
Research Area Signaling, Phospho-specific antibodies, Protein Modifications, Chromatin, Metabolism, Cell Structure
Application Notes The suggested dilution is: WB: = 1:10000-50000
Comment

Background: Acetyl-CoA carboxylase 1 (ACC1) is a biotin dependent lipogenic enzyme that is highly expressed during adipogenesis. ACC1 catalyzes acetyl-CoA carboxylation, producing malonyl-CoA, a metabolite involved in energy homeostasis regulation. Malonyl-CoA is a two carbon donor in the synthesis of long-chain fatty acids and the elongation of fatty acids found in the cystol (1). ACC1 is regulated short-term by citrate, CoA, and palmitoyl-CoA through allosteric interactions. Nutrients and hormones can be both short-term (inducing reversible phosphorylations by such as AMPK at Ser79 and others) and long-term (transcription level regulation) regulators of ACC1 (2). Highly expressed in lipogenic tissues, ACC1 is found in liver, adipose, and lactating mammary gland (3). ACC1 has been implicated as a target in the development of anti-obesity drugs (4).

Restrictions For Research Use only
Format Liquid
Buffer 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Storage Comment Acetyl-CoA1 (ACC1) Antibody Phospho-pS79 can be stored at -20°C for up to 12 months from time of receipt.
Expiry Date 12 months
Background publications Wakil, Stoops, Joshi: "Fatty acid synthesis and its regulation." in: Annual review of biochemistry, Vol. 52, pp. 537-79, 1983 (PubMed).

Abu-Elheiga, Matzuk, Abo-Hashema et al.: "Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2." in: Science (New York, N.Y.), Vol. 291, Issue 5513, pp. 2613-6, 2001 (PubMed).

Mao, Chirala, Wakil: "Human acetyl-CoA carboxylase 1 gene: presence of three promoters and heterogeneity at the 5'-untranslated mRNA region." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 100, Issue 13, pp. 7515-20, 2003 (PubMed).

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