Merck Anti-AMPK α1 Antibody

Anti-AMPK α1 Antibody

Upstate®, from rabbit

5′-AMP-activated protein kinase, catalytic alpha-1 chain, AMP -activate kinase alpha 1 subunit, AMP-activated protein kinase, catalytic, alpha-1, AMPK alpha 1, AMPK alpha-1 chain, protein kinase, AMP-activated, alpha 1 catalytic subunit

5′-AMP-activated protein kinase catalytic subunit alpha-1 (UniProt: Q13131; also known as EC:2.7.11.1, AMPK subunit alpha-1, Acetyl-CoA carboxylase kinase, ACACA kinase, Hydroxymethylglutaryl-CoA reductase kinase, HMGCR kinase, Tau-protein kinase PRKAA1) is encoded by the PRKAA1 (also known as AMPK1) gene (Gene ID: 5562) in human.AMPK is a heterotrimer composed of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). It also contains an autoinhibitory sequence that shows some sequence similarity with the ubiquitin-associated domains and it represses kinase activity. AMPK is 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, including inhibition of protein, carbohydrate and lipid biosynthesis, and reduces cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. AMPK is shown to regulate insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 and it stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter GLUT4 to the plasma membrane. In the liver it acts as a key regulator of glucose homeostasis by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. AMPK is activated by phosphorylation on Thr183. Binding of AMP to non-catalytic gamma subunit results in allosteric activation, inducing phosphorylation on Thr183. AMP-binding to gamma subunit also sustains activity by preventing dephosphorylation of Thr183.