抗Human PRKAB2 抗体:
抗Mouse (Murine) PRKAB2 抗体:
抗Rat (Rattus) PRKAB2 抗体:
Human Polyclonal PRKAB2 Primary Antibody for IHC (p), ELISA - ABIN545500
Park, Paulsen, Gammon, Mustard, Hardie, Winder: Effects of thyroid state on AMP-activated protein kinase and acetyl-CoA carboxylase expression in muscle. in Journal of applied physiology (Bethesda, Md. : 1985) 2002
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Cow (Bovine) Polyclonal PRKAB2 Primary Antibody for WB - ABIN2786810
Ewing, Chu, Elisma, Li, Taylor, Climie, McBroom-Cerajewski, Robinson, OConnor, Li, Taylor, Dharsee, Ho, Heilbut, Moore, Zhang, Ornatsky, Bukhman, Ethier, Sheng, Vasilescu, Abu-Farha, Lambert, Duewel et al.: Large-scale mapping of human protein-protein interactions by mass spectrometry. ... in Molecular systems biology 2007
AMP-activated protein kinase can be modulated by diverse ligands and by phosphorylation.
Sleep disturbances are one of the most common problems affecting individuals with psychiatric disorders. We show that AMPK is required for maintenance of proper sleep architecture and for sleep recovery following sleep deprivation. Neuronal AMPKbeta loss specifically leads to sleep fragmentation and causes dysregulation of genes believed to play a role in sleep homeostasis.
Sumoylation of AMPKbeta2 subunit enhances AMP-activated protein kinase activity.
Data indicate that except AMPK-alpha1, expressions of the other five AMPK subunits -alpha2, -beta1, -beta2, -gamma1 and -gamma2 are significantly higher in ovarian carcinomas.
Studies suggest insights into the regulation of AMPK, its diverse biological actions, and therapeutic potential in the heart.
results of this study demonistrated that the novel findings that intronic SNPs in the genes coding for the regulatory beta2(PRKAB2) of AMPK are associated with antipsychotic-induced weight gain in schizophrenia or schizoaffective disorder patients
These results suggest that the modification introduced by the laforin-malin complex could affect the subcellular distribution of AMPK beta subunits.
Purification and characterization of truncated human AMPK alpha 2 beta 2 gamma 3 heterotrimer from baculovirus-infected insect cells
variants in PRKAB2 are unlikely to contribute to the type 2 diabetes mellitus susceptibility in Pima Indians
the evidence indicates that AMPK is sufficient but not essential for the maintenance of DAPC expression in skeletal muscle, yet it is required for preserving extrasynaptic utrophin levels in slow oxidative muscles.
AMPK directly relaxes vascular smooth muscle cell by a decrease of [Ca(2+)]i. This is achieved by calcium sequestration via SERCA activation, as well as activation of BKCa channels.
AMPK beta1beta2 have a role in preventing myopathy due to loss of capillary density in nonpostural muscles
The beta2 subunit plays an important role in regulating glucose, glycogen, and lipid metabolism during metabolic stress. beta2 mutant animals failed to maintain euglycemia and muscle ATP levels during fasting.
Data show that beta1beta2M-KO mice are physically inactive and have a drastically impaired capacity for treadmill running that is associated with reductions in skeletal muscle mitochondrial content.
Deletion of AMPK beta2 reduces AMPK activity in skeletal muscle resulting in impaired exercise capacity.
Germline deletion of either AMPK beta1 or beta2 subunit isoforms resulted in reduced trabecular bone density and mass, but without effects on osteoclast (OC) or osteoblast (OB) numbers.
Results suggest that p38 MAPK is not a downstream component of AMPK-mediated signaling in skeletal muscle.
The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. It is highly expressed in skeletal muscle and thus may have tissue-specific roles.
protein kinase, AMP-activated, beta 2 non-catalytic subunit
, AMP-activated protein kinase beta 2 non-catalytic subunit
, 5'-AMP-activated protein kinase subunit beta-2
, 5'-AMP-activated protein kinase, beta-2 subunit
, AMPK beta 2
, AMPK beta-2 chain
, AMPK subunit beta-2
, AMP-activated protein kinase beta-2 regulatory subunit
, AMPK beta-2