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Biochem/physiol Actions
PRKAG2 (protein kinase, AMP-activated, γ2 non-catalytic subunit) acts as a sensor of cellular energy status that is controlled by AMP (positively) and ATP (negatively). In normal state CBS domains from AMP-activated protein kinase can bind AMP, ATP, or S-adenosyl methionine. But in mutated condition, it cannot bind. As a result, it leads to hereditary diseases. Its major activity is involved in the regulation of energy homeostasis. It plays an important role in correcting of cell division and chromosome segregation during mitosis. Mutation in PRKAG2 causes Wolff-Parkinson-White (WPW) syndrome, a rare autosomal dominant inheritance disease.
General description
AMP-activated protein kinase (AMPK) is a heterotrimeric protein composed of a catalytic alpha subunit, a noncatalytic beta subunit, and a noncatalytic regulatory gamma subunit. Various forms of each of these subunits exist, encoded by different genes. AMPK is an important energy-sensing enzyme that monitors cellular energy status and functions by inactivating key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This gene is a member of the AMPK gamma subunit family and encodes a protein with four cystathionine beta-synthase domains. Mutations in this gene have been associated with ventricular pre-excitation (Wolff-Parkinson-White syndrome), progressive conduction system disease and cardiac hypertrophy. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. (provided by RefSeq)
Immunogen
PRKAG2 (NP_077747.1, 1 a.a. ~ 328 a.a) full-length human protein.SequenceMLEKLEFEDEAVEDSESGVYMRFMRSHKCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETWRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFLQLFMSDMPKPAFMKQNLDELGIGTYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALILTPAGAKQKETETE
Physical form
Solution in phosphate buffered saline, pH 7.4
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