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anti-Rat (Rattus) PRKAG3 Antibodies:
anti-Human PRKAG3 Antibodies:
anti-Mouse (Murine) PRKAG3 Antibodies:
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Cow (Bovine) Polyclonal PRKAG3 Primary Antibody for ELISA - ABIN451738
Costford, Kavaslar, Ahituv, Chaudhry, Schackwitz, Dent, Pennacchio, McPherson, Harper: Gain-of-function R225W mutation in human AMPKgamma(3) causing increased glycogen and decreased triglyceride in skeletal muscle. in PLoS ONE 2007
Human Polyclonal PRKAG3 Primary Antibody for IHC (p), ELISA - ABIN545505
Fukuyama, Ohta, Okoshi, Suehara, Kizaki, Nakagawa: Hypoxia induces expression and activation of AMPK in rat dental pulp cells. in Journal of dental research 2007
Alleles of 2 equine AMPK gamma subunit genes had no causative role in polysaccharide storage myopathy in horses
PRKAG3-230 may be associated with sporadic Wolff-Parkinson-White (WPW) syndrome in a Taiwanese population.
The mTOR pathway was significantly associated with overall and estrogen receptor-negative (ER-) breast cancer risk (P = 0.003 and 0.03, respectively). PRKAG3 (Padj = 0.0018) and RPS6KA3 (Padj = 0.061) were the leading genes for the associations with overall breast cancer risk and ER- breast cancer risk, respectively.
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.
Low PRKAA2 expression is associated with follicular lymphoma.
Through the enhancement of skeletal muscle glucose uptake and increased mitochondrial content, the R225W mutation of the gene encoding AMP-activated protein kinase (AMPK)gamma(3)may significantly enhance exercise performance.
Purification and characterization of truncated human AMPK alpha 2 beta 2 gamma 3 heterotrimer from baculovirus-infected insect cells
identified for the first time a mutation in the skeletal muscle-specific regulatory gamma(3) subunit of AMPK in humans
the observation that the AMPKgamma3 isoform is expressed primarily in white skeletal muscle, in which it is the predominant gamma-isoform, strongly suggests that gamma3 has a key role in this tissue
role of the AMPKgamma3 isoform in exercise-induced metabolic and gene regulatory responses in skeletal muscle
data show that different mutations in gamma3 exert different effects on allosteric regulation of alpha2beta2gamma3 complex by AMP, whereas we find no evidence for their role in regulating the level of phosphorylation of alpha2 by upstream kinases.
Genetic variability in PRKAG3 does not seem to have a major effect on glucose metabolism, but play a role in lipoprotein metabolism in humans.
Variants in genes for AMPKalpha2 and AMPKgamma3 were not associated with PCOS or its component traits.
Functional analysis of the pig counterpart.
Association between polymorphism in bovine PRKAG3 gene and milk production traits.
Activity of glycogen synthase without the allosteric activator glucose 6-phosphate was decreased in gain of function AMPKgamma3(R200Q) relative to all other genotypes
Greater net lactate accumulation postmortem (i.e., glycolytic flux) coupled with a lower buffering capacity explains the lower ultimate pH of meat from AMPKgamma3(R200Q) mutant pigs.
allelic frequencies of PRKAG3 in several pig breeds
The variation in the promoter region of the porcine PRKAG3 gene has associations with meat quality phenotypes, including traits which are influenced by glycolytic potential and muscle metabolism in a breed-dependent manner.
PRKAG3 mutation influences muscle characteristics and promotes an oxidative phenotype to a varying degree among muscles with different functions
increased rate of glycogen synthesis following exercise in pigs carrying the PRKAG3 mutation correlates with an increased signalling response of Akt and its substrate, AS160.
Genetic variation of PRKAG3 was studied in indigenous breeds of China.
the R225Q mutation of PRKAG3 is associated with higher basal AMPK activity and diminished AMP dependence
findings suggest that the R200Q mutation results in a constitutively active enzyme, leading to hyperaccumulation of glycogen due to the increased influx of glucose
Data suggest that the AMPK-TBC1D4 signaling axis is likely mediating the improved muscle insulin sensitivity after contraction/exercise and illuminates an important and physiologically relevant role of AMPK in skeletal muscle.
The AMPKgamma3 isoform is dispensable for functional overload-induced muscle growth.
gamma3-AMPK down-regulation is a rapid physiological muscle response observed in mouse after running exercise or fasting, two situations leading to PPARbeta activation.
AMPK acts as the primordial trigger for fasting- and exercise-induced adaptations in skeletal muscle and that activation of SIRT1 and its downstream signaling pathways are improperly triggered in AMPK-deficient states.
subunit R225Q mutation effect on growth performance with normal or high-energy diet
Gamma3 subunit of AMPK is highly expressed in fast-twitch glycolytic skeletal muscle, and wild-type gamma3 functions in the regulation of alpha1 catalytic activity, but it is not associated with changes in muscle glycogen concentrations
functional studies of the protein kinase, AMP-activated, gamma 3 (AMPK3) isoform further support the close connection between glycogen content and exercise performance in skeletal muscle
AMPKg3 is involved in the coordinated transcription of genes critical for lipid and glucose metabolism in white glycolytic skeletal muscle.
analysis of transcriptional regulation in skeletal muscle of AMP-activated protein kinase gamma3 R225Q transgenic and knock-out mice
Expression of either wild type or mutant (R225Q) gamma3-subunit of AMPK results in increased glycogen concentrations in muscle, but the mechanisms underlying this alteration appear to be different.
AMPK heterotrimeric complexes containing the AMPKgamma(3) subunit may play a specific role in linking circadian oscillators and energy metabolism in skeletal muscle.
Basal and A-769662-mediated IL-6 release provide evidence for a role of AMPK in the regulation of IL-6 release from oxidative skeletal muscle.
AMPK gamma3 subunit is associated with mitochondrial biogenesis in glycolytic skeletal muscle, concomitant with increased expression of the co-activator PGC-1alpha and several transcription factors that regulate mitochondrial proteins
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. It is dominantly expressed in skeletal muscle. Studies of the pig counterpart suggest that this subunit may play a key role in the regulation of energy metabolism in skeletal muscle.
5'-AMP-activated protein kinase subunit gamma-3
, AMP-activated protein kinase gamma 3 subunit
, protein kinase, AMP-activated, gamma 3 non-catatlytic subunit
, 5'-AMP-activated protein kinase gamma-3 non-catalytic subunit long form
, AMP-activated protein kinase gamma subunit
, protein kinase non-catalytic gamma subunit
, AMP-activated protein kinase, non-catalytic gamma-3 subunit
, AMP-activated protein kinase gamma 3
, AMPK-activated protein kinase gamma-3 subunit
, protein kinase, AMP-activated, gamma 3 non-catalytic subunit a
, protein kinase, AMP-activated, gamma 3 non-catalytic subunit
, AMP-activated protein kinase subunit gamma
, 5'-AMP-activated protein kinase subunit gamma-3-like
, 5'-AMP-activated protein kinase, gamma-3 subunit
, AMPK gamma-3 chain
, AMPK gamma3
, AMPK subunit gamma-3
, 5'-AMP-activated protein kinase gamma-3 subunit
, AMP-activated protein kinase gamma