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Recombinant full-length human AMPK (combination of A1/B1/G1 subunits) was expressed by baculovirus in Sf9 insect cells using C-terminal His tags. AMPK is a heterotrimeric protein kinase consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated and phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating biosynthesis of fatty acid and cholesterol. ADP-Glo Kinase Assay is a luminescent kinase assay that measures ADP formed from a kinase reaction; ADP is converted into ATP, which is a substrate in a reaction catalyzed by Ultra-Glo Luciferase that produces light. The luminescent signal positively correlates with ADP amount and kinase activity. The assay is well suited for measuring the effects chemical compounds have on the activity of a broad range of purified kinases, making it ideal for both primary screening as well as kinase selectivity profiling. The ADP-Glo Kinase Assay can be used to monitor the activity of virtually any ADP-generating enzyme (e.g., kinase or ATPase) using up to 1mM ATP. Kinase Enzyme System contains: Kinase: AMPK (A1/B1/G1), 10ug (Human, recombinant full-length). MW: ~68kDa (A1); ~38kDa (B1); ~40kDa (G1). Substrate: SAMStide (HMRSAMSGLHLVKRR); derived from mouse acetyl-Coenzyme A carboxylase alpha (amino acid 73-85). Other: Reaction Buffer, DTT, AMP Solution. AMPK (A1/B1/G1) NCBI Database Entry: www.ncbi.nlm.nih.gov/gene/5562/. Visit www.promega.com/kinase/ to see all Kinase Enzyme Systems.