AMPK (A1/B2/G1) is a member of the AMPK family which are heterotrimeric proteins consisting of an α catalytic subunit, and non-catalytic β and γ subunits. AMPKs are an important energy-sensing enzyme group in the cells that monitor energy status particularly in response to stress. AMPKs regulate fatty acid and cholesterol synthesis by regulating the key rate-limiting enzymes acetyl-CoA carboxylase and 3-hydroxy-3-methylglutaryl-CoA reductase. The β subunit may be a positive regulator of AMPK activity and is highly expressed in skeletal muscle.
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Supplied in 50 mM Sodium Phosphate, pH 7.0, with 150 mM imidazole, 0.1 mM PMSF, 0.2 mM DTT, and 25% glycerol.
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The Journal of biological chemistry, 273(20), 12443-12450 (1998-06-20)
The AMP-activated protein kinase (AMPK) is a member of a growing family of related kinases, including the SNF1 complex in yeast, which respond to nutritional stress. AMPK is a heterotrimeric complex of a catalytic subunit (alpha) and two regulatory subunits
Biochemical Society transactions, 31(Pt 1), 216-219 (2003-01-28)
AMP-activated protein kinase (AMPK) is viewed as a fuel sensor for glucose and lipid metabolism. To understand better the physiological role of the catalytic AMPK subunit isoforms, we generated two knockout mouse models with the alpha1 (AMPK alpha 1(-/-)) and
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