AMPK gamma 1/beta 1/alpha 1 Heterotrimer Protein, Human (Active, sf9, His)

The AMPK gamma 1/beta 1/alpha 1 heterotrimer serves as the AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), a pivotal regulator of cellular energy metabolism. When intracellular ATP levels decrease, AMPK is activated, initiating a cascade of events that enhance energy production while suppressing energy-consuming processes such as protein, carbohydrate, and lipid biosynthesis, as well as cell growth and proliferation. The gamma non-catalytic subunit of AMPK mediates binding to AMP, ADP, and ATP, influencing the activation or inhibition of AMPK. AMP binding allosterically activates the alpha catalytic subunit by inducing phosphorylation and preventing dephosphorylation. ADP stimulates phosphorylation, while ATP promotes dephosphorylation, rendering the AMPK enzyme inactive. Beyond its role in energy regulation, AMPK acts as a modulator of cellular polarity by remodeling the actin cytoskeleton, potentially through the indirect activation of myosin. The heterotrimeric composition of AMPK includes an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta subunit (PRKAB1 or PRKAB2), and a gamma non-catalytic subunit (PRKAG1, PRKAG2, or PRKAG3), highlighting its intricate regulatory mechanisms. AMPK further interacts with FNIP1 and FNIP2 to modulate its cellular functions.