This product is an active protein and may elicit a biological response in vivo, handle with caution.
5 AMP activated protein kinase alpha 1catalytic subunit
5 AMP activated protein kinase catalytic alpha 1 chain
5 AMP activated protein kinase subunit gamma 3
5' AMP activated protein kinase beta 2 subunit
5' AMP activated protein kinase catalytic subunit alpha 1
5' AMP activated protein kinase catalytic subunit alpha-1
5' AMP activated protein kinase subunit beta 2
5' AMP activated protein kinase subunit beta-2
Acetyl CoA carboxylase kinase
AMP -activate kinase alpha 1 subunit
AMP activated protein kinase beta 2 non catalytic subunit
AMP-activated protein kinase, catalytic, alpha -1
AMP-activated protein kinase, catalytic, alpha1
AMPK alpha 1
AMPK alpha 1 chain
AMPK beta 2
AMPK beta 2 chain
AMPK gamma 3
AMPK gamma 3 chain
AMPK subunit alpha 1
AMPK subunit alpha-1
AMPK subunit gamma 3
AMPK subunit gamma3
HMG CoA reductase kinase
Hormone sensitive lipase kinase
Kinase AMPK alpha1
Protein kinase AMP activated alpha 1 catalytic subunit
Protein kinase AMP activated beta 2 non catalytic subunit
Protein kinase AMP activated gamma 3 non catalytic subunit
SNF1-like protein AMPK
Tau protein kinase PRKAA1
AMPK alpha 1: Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic subunit.
AMPK beta 2: AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. Also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase and hormone-sensitive lipase. This is a regulatory subunit, may be a positive regulator of AMPK activity. It may also serve as an adapter molecule for the catalytic alpha-subunit.
AMPK gamma 3: 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.
Cytoplasmic and Nuclear
Functional Studies - Active human AMPK alpha 1 + AMPK beta 2 + AMPK gamma 3 full length protein (ab184885)
Kinase Assay demonstrating specific activity of ab184885.