The antiserum was produced against synthesized peptide derived from human AMPK alpha around the phosphorylation site of Thr172. AA range:140-189

This antibody detects endogenous AMPKα1 only when phosphorylated at threonine 183 and endogenous AMPKα2 only when phosphorylated at threonine 172. The antibody does not detect the regulatory β or γ subunits.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):LRtSC

AAPK1/AAPK2

5'-AMP-activated protein kinase catalytic subunit alpha-1/2

PRKAA1 ;
AMPK1 ;
5'-AMP-activated protein kinase catalytic subunit alpha-1 ;
AMPK subunit alpha-1 ;
Acetyl-CoA carboxylase kinase ;
ACACA kinase ;
Hydroxymethylglutaryl-CoA reductase kinase ;
HMGCR kinase ;
Tau-protein kinase PRKAA1 ;
PRKAA2 ;
AMPK ;

The protein encoded by this gene belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008],

Catalytic activity:ATP + a protein = ADP + a phosphoprotein.,cofactor:Magnesium.,enzyme regulation:Binding of AMP results in allosteric activation, inducing phosphorylation on Thr-174 by STK11 in complex with STE20-related adapter-alpha (STRAD alpha) pseudo kinase and CAB39. Also activated by phosphorylation by CAMKK2 triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio.,Function: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.,sequence Caution:Translation N-terminally shortened.,similarity:Belongs to the protein kinase superfamily.,similarity:Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.,similarity:Contains 1 protein kinase domain.,subunit:Heterotrimer of an alpha catalytic subunit, a beta and a gamma non-catalytic subunits. Interacts with FNIP1 and FNIP2.,

Cytoplasm . Nucleus . In response to stress, recruited by p53/TP53 to specific promoters. .

>>FoxO signaling pathway ;
>>Autophagy - animal ;
>>mTOR signaling pathway ;
>>PI3K-Akt signaling pathway ;
>>AMPK signaling pathway ;
>>Longevity regulating pathway ;
>>Longevity regulating pathway - multiple species ;
>>Apelin signaling pathway ;
>>Tight junction ;
>>Circadian rhythm ;
>>Thermogenesis ;
>>Insulin signaling pathway ;
>>Adipocytokine signaling pathway ;
>>Oxytocin signaling pathway ;
>>Glucagon signaling pathway ;
>>Insulin resistance ;
>>Non-alcoholic fatty liver disease ;
>>Alcoholic liver disease ;
>>Hypertrophic cardiomyopathy ;
>>Fluid shear stress and atherosclerosis