AMPK (G1/B2/A2) Heterotrimer Protein (recombinant human)

Activity: The specific activity was determined to be 6 nmol/min/mg using synthetic SAMS peptide (HMRSAMSGLHLVKRR) as substrate. Protein Construction: A DNA sequence encoding the human PRKAG1 (P54619) (Met 1-Pro 331), constructed the plasmid 1, A DNA sequence encoding the human PRKAB2 (O43741) (Met 1-Ile 272), constructed the plasmid 2, A DNA sequence encoding the human PRKAA2 (P54646) (Met 1-Arg 552) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus, constructed the plasmid 3. The three plasmids were co-expressed and the heterotrimer was purified. Sequence: Met 1-Pro 331. Endotoxin: < 1.0 EU per µg of the protein as determined by the LAL method. Apparent Molecular Mass: 35, 37 & 95 kDa. Protein function: Protein function: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton, probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive. [The UniProt Consortium]