The 5-AMP-activated protein kinase (AMPK) is a member of the SNF1 (sucrose nonfermentor) kinase family (1). AMPK is a heterotrimeric protein comprising α (63 kDa), β (38 kDa) and γ (38 kDa) subunits (2). The alpha subunit is the catalytic subunit, while beta and gamma are noncatalytic subunits, although they have been found to interact with the active subunit in liver. AMPK regulates fatty acid and sterol synthesis by phosphorylation of acetyl-CoA, as well as cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (3). AMPK beta-1 mediates the association of the AMPK heterotrimeric complex in vitro (2). Two isoforms have been found, and the difference in expression patterns indicates tissue-specific roles for these isoforms (4).
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