• Nature
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
    • Sequence
    • Amino acids
      191 to 300
    • Tags
      GST tag N-Terminus


Our Abpromise guarantee covers the use of ab162545 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications


    Western blot

  • Form
  • Additional notes
    Protein concentration is above or equal to 0.05 mg/ml.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.31% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names
    • 5''-AMP-activated protein kinase subunit gamma-2
    • AAKG
    • AAKG2
    • AMPK gamma2
    • AMPK subunit gamma 2
    • AMPK subunit gamma-2
    • CMH6
    • H91620p
    • Prkag2
    • Protein kinase AMP activated gamma 2 non catalytic subunit
    • WPWS
    see all
  • 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.
  • Tissue specificity
    Isoform B is ubiquitously expressed except in liver and thymus. The highest level is detected in heart with abundant expression in placenta and testis.
  • Involvement in disease
    Defects in PRKAG2 are the cause of Wolff-Parkinson-White syndrome (WPWS) [MIM:194200]; also known as preexcitation syndrome. It is the second most common cause of paroxysmal supraventricular tachycardia.
    Defects in PRKAG2 are the cause of cardiomyopathy, familial hypertrophic type 6 (CMH6) [MIM:600858]. A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. CMH6 patients present Wolff-Parkinson-White ventricular preexcitation, enlarged myocytes without myofiber disarray, and glycogen-containing cytosolic vacuoles within cardiomyocytes.
    Defects in PRKAG2 are a cause of glycogen storage disease of heart lethal congenital (GSDH) [MIM:261740]; also known as phosphorylase kinase deficiency of heart or congenital nonlysosomal cardiac glycogenosis. GSDH is a rare disease which leads to death within a few weeks to a few months after birth, through heart failure and respiratory compromise.
  • Sequence similarities
    Belongs to the 5'-AMP-activated protein kinase gamma subunit family.
    Contains 4 CBS domains.
  • Domain
    The AMPK pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins of AMPK, except the presence of a non-phosphorylatable residue in place of Ser. In the absence of AMP this pseudosubstrate sequence may bind to the active site groove on the alpha subunit (PRKAA1 or PRKAA2), preventing phosphorylation by the upstream activating kinase STK11/LKB1.
    The CBS domains mediate binding to AMP, ADP and ATP. 2 sites bind either AMP or ATP, whereas a third site contains a tightly bound AMP that does not exchange. Under physiological conditions AMPK mainly exists in its inactive form in complex with ATP, which is much more abundant than AMP.
  • Post-translational
    Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK. Phosphorylated upon DNA damage, probably by ATM or ATR.
  • Information by UniProt


  • ab162545 on a 12.5% SDS-PAGE stained with Coomassie Blue.


ab162545 has not yet been referenced specifically in any publications.

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