A6986
Acetyl-CoA Carboxylase 1 human
recombinant, expressed in Sf9 cells
Sinónimos:
ACAC, ACACA, ACC, ACC1, ACCA, acetyl-CoA carboxylase alpha
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Descripción general
Acetyl-CoA Carboxylase 1 (ACACA) is mapped to human chromosome 17q12.[1] It is majorly expressed in liver and adipose tissue.[2] ACACA has biotin carboxylase (BC), biotin carboxyl carrier protein (BCCP) and carboxyl transferase (CT) domains and an additional interaction domain. (BT) A central domain region (CD) connects the BC and CT domains.[3] ACACA is a key regulator of energy balance. The ACACA catalysis is the rate-limiting step in the synthesis of malonyl-CoA and regulation of free fatty acid oxidation.[2] Elevated levels of ACACA contributes to obesity and tumor progression.[3]
Formulation: Solution in Tris-HCl (pH 8), NaCl, Glycerol
Aplicación
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Acciones bioquímicas o fisiológicas
Acetyl-CoA Carboxylase (ACC) catalyzes the formation of Malonyl CoA through the irreversible carboxylation of acetyl CoA. ACC is activated by citrate, glutamate, and dicarboxylic acids and negatively regulated by long- and short chain-fatty acyl-CoAs. ACC1 is essential for breast cancer and prostrate cancer cell survival.
Acetyl-CoA Carboxylase (ACC) regulates the metabolism of fatty acids. This enzyme catalzes the formation of Malonyl CoA through the irreversible carboxylation of acetyl CoA. There are two main isoforms of Acetyl-CoA carboxylase expressed in mammals, Acetyl-CoA carboxylase 1 (ACACA) and Acetyl-CoA carboxylase 2 (ACACB). ACACA has broad tissue distribution but is enriched in tissues critical for fatty acid sythesis such as adipose tissue. ACACB is enriched in tissues such as skeletal muscle and heart that are critical for fatty acid oxidation.
The Acetyl-CoA Carboxylase enzymes are activated by citrate, glutamate, and dicarboxylic acids and negatively regulated by long and short chain fatty acyl CoAs. Acetyl-CoA Carboxylase 1 is essential for breast cancer and prostrate cancer cell survival. Because of thier roles in fatty acid metabolism and oxidation, ACACA and ACACB are therapeutic targets for treating obesity and metabolic syndrome disorders.
The Acetyl-CoA Carboxylase enzymes are activated by citrate, glutamate, and dicarboxylic acids and negatively regulated by long and short chain fatty acyl CoAs. Acetyl-CoA Carboxylase 1 is essential for breast cancer and prostrate cancer cell survival. Because of thier roles in fatty acid metabolism and oxidation, ACACA and ACACB are therapeutic targets for treating obesity and metabolic syndrome disorders.
Propiedades físicas
α transcript variant 1, C-terminal histidine-tagged 270 kDa protein containing amino acids 1-2383 (end)
Definición de unidad
One unit will cause the conversion of 1 picomole of ATP to ADP per minute at pH 7.4 at 30 °C
Nota de preparación
Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.
Código de clase de almacenamiento
12 - Non Combustible Liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
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Structural basis for regulation of human acetyl-CoA carboxylase
Hunkeler M, et al.
Nature, 558, 470-474 (2018)
Regulation of acetyl CoA carboxylase and carnitine palmitoyl transferase-1 in rat adipocytes
Zang Y, et al.
Obesity Research, 13(9), 1530-1539 (2005)
Graeme J Gowans et al.
Cell metabolism, 18(4), 556-566 (2013-10-08)
While allosteric activation of AMPK is triggered only by AMP, binding of both ADP and AMP has been reported to promote phosphorylation and inhibit dephosphorylation at Thr172. Because cellular concentrations of ADP and ATP are higher than AMP, it has
Jorgen F P Wojtaszewski et al.
American journal of physiology. Endocrinology and metabolism, 284(4), E813-E822 (2002-12-19)
The metabolic role of 5'AMP-activated protein kinase (AMPK) in regulation of skeletal muscle metabolism in humans is unresolved. We measured isoform-specific AMPK activity and beta-acetyl-CoA carboxylase (ACCbeta) Ser(221) phosphorylation and substrate balance in skeletal muscle of eight athletes at rest
Pietro Palumbo et al.
Gene, 538(2), 373-378 (2014-02-04)
Microdeletions of 17q12 including the hepatocyte nuclear factor 1 beta (HNF1B) gene, as well as point mutations of this gene, are associated with the Renal Cysts and Diabetes syndrome (RCAD, OMIM 137920) and genitourinary alterations. Also, microdeletions encompassing HNF1B were
Artículos
Fatty acid synthesis supports cancer cell proliferation, essential for membrane generation, protein modification, and bioenergetics.
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