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anti-Human PRKAG1 Antibodies:
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Human Monoclonal PRKAG1 Primary Antibody for IHC, ELISA - ABIN1724935
Zaha, Young: AMP-activated protein kinase regulation and biological actions in the heart. in Circulation research 2012
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Human Monoclonal PRKAG1 Primary Antibody for ICC, FACS - ABIN1724932
Oliveira, Zhang, Solis, Isackson, Bellahcene, Yavari, Pinter, Davies, Ge, Ashrafian, Walker, Carling, Watkins, Casadei, Redwood: AMP-activated protein kinase phosphorylates cardiac troponin I and alters contractility of murine ventricular myocytes. in Circulation research 2012
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Human Polyclonal PRKAG1 Primary Antibody for IHC (p), ELISA - ABIN545503
Zidovetzki, Wang, Chen, Jeyaseelan, Hofman: Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways. in AIDS research and human retroviruses 1998
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AMPK activity in response to redox changes is not due to direct action on AMPK itself, but is a secondary consequence of redox effects on other processes, such as mitochondrial ATP production.
AMP-activated protein kinase can be modulated by diverse ligands and by phosphorylation.
Data suggest different gamma-isoforms in AMPK can have different effects on enzyme activation; here, activation of AMPK by compound 991 is greater if AMPK contains PRKAG2 versus PRKAG1 or PRKAG3.
A subunit composition of AMPK (alpha2beta2gamma1) is preferred for colorectal cancer cell survival, at least in part, by stabilizing the tumor-specific expression of PGC1B.
Pin1 plays an important role in the pathogenic mechanisms underlying impaired glucose and lipid metabolism, functioning as a negative regulator of AMPK
Letter: report PRKAG1 frameshift mutations in colorectal cancer.
Electrogenic phosphate transport in sodium/phosphate cotransporter NaPi-IIa-expressing Xenopus oocytes is markedly decreased by the coexpression of constitutively active AMPKgammaR70Q, but not of AMPK(alphaK45R).
PRKAG1 interacts with DSCAM through its gamma subunit, and netrin-1 activates AMPK phosphorylation in cortical neurons.
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.
In breast cancer cells SESN2 is associated with AMPK.
Conclude that cTnI phosphorylation by AMPK may represent a novel mechanism of regulation of cardiac function.
Studies indicate that in most species, AMPK exists as an obligate heterotrimer, containing a catalytic subunit (alpha), and two regulatory subunits (beta and gamma).
Findings reveal that hypoxia can trigger AMPK activation in the apparent absence of increased [AMP] through ROS-dependent CRAC channel activation, leading to increases in cytosolic calcium that activate the AMPK upstream kinase CaMKKbeta.
Results suggest that AMPK association with ULK1 plays an important role in autophagy induction.
findings show that that a beta1(186-270)gamma1 complex can form in the absence of detectable alpha subunit and that beta1 Thr-263 and Tyr-267 are required for betagamma association but not alphabeta association
Inhibition of the KCa3.1 channels by AMP-activated protein kinase in human airway epithelial cells.
AMP-activated protein kinase inhibits alkaline pH- and PKA-induced apical vacuolar H+-ATPase accumulation in epididymal clear cells.
These results emphasize the clinical relevance of activating AMPK in the liver to combat non-alcoholic fatty liver disease.
Transgenic activation of skeletal muscle AMPKgamma1 in this model plays an important sex-specific role in skeletal muscle metabolism and whole body energy homeostasis.
Data indicate that a diet high in iron improves glucose tolerance by activating AMPK through mechanisms that include deacetylation.
Results demonstrate that AMPKgamma1 subunit is required for the maintenance of erythrocyte membrane elasticity.
In R70Qgamma1-expressing mice, there is an increase in muscle glycogen synthase activity associated with an increase in exercise capacity.
AMPK is not necessary for exercise training-induced increases in mitochondrial markers, but it is essential for fiber type IIb to IIa/x transformation and increases in hexokinase II protein[AMP-activated protein kinase gamma1]
mapped on porcine chromosome 5
isolation and characterization of the gene for the noncatalytic bovine gamma1 subunit of AMPK
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 is one of the gamma regulatory subunits of AMPK. Alternatively spliced transcript variants encoding distinct isoforms have been observed.
protein kinase, AMP-activated, gamma 1 non-catalytic subunit
, 5'-AMP-activated protein kinase subunit gamma-1
, AMPK-activated protein kinase gamma-1 subunit
, AMP-activated protein kinase, noncatalytic gamma-1 subunit
, 5'-AMP-activated protein kinase subunit gamma-1-like
, 5'-AMP-activated protein kinase, gamma-1 subunit
, AMPK gamma-1 chain
, AMPK gamma1
, AMPK subunit gamma-1
, Protein kinase AMP-activated gamma
, 38 kDa subunit
, 5'-AMP-activated protein kinase gamma-1 subunit
, AMP-activated protein kinase subunit gamma 1 (non-catalytic subunit)