|Other Names||5'-AMP-activated protein kinase subunit gamma-1, AMPK gamma1, AMPK subunit gamma-1, AMPKg, PRKAG1|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|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.|
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The protein encoded by this gene belongs to thephosphoinositide 3-kinase (PI3K) family. PI3-kinases play roles insignaling pathways involved in cell proliferation, oncogenictransformation, cell survival, cell migration, and intracellularprotein trafficking. This protein contains a lipid kinase catalyticdomain as well as a C-terminal C2 domain, a characteristic of classII PI3-kinases. C2 domains act as calcium-dependent phospholipidbinding motifs that mediate translocation of proteins to membranes,and may also mediate protein-protein interactions. The PI3-kinaseactivity of this protein is not sensitive to nanomolar levels ofthe inhibitor wortmanin. This protein was shown to be able to beactivated by insulin and may be involved in integrin-dependentsignaling.
Liu, C.Y., et al. Carcinogenesis 31(7):1259-1263(2010)Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Kostakis, G.C., et al. Oral Surg Oral Med Oral Pathol Oral Radiol Endod 109 (5), E53-E58 (2010) :Koutros, S., et al. Cancer Res. 70(6):2389-2396(2010)Ng, S.K., et al. Biochem. Biophys. Res. Commun. 387(2):310-315(2009)
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