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anti-Human PRKAA2 Antibodies:
anti-Rat (Rattus) PRKAA2 Antibodies:
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Cow (Bovine) Polyclonal PRKAA2 Primary Antibody for WB - ABIN151705
Rubin, Magliola, Feng, Jones, Hale: Metabolic activation of AMP kinase in vascular smooth muscle. in Journal of applied physiology (Bethesda, Md. : 1985) 2004
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Human Polyclonal PRKAA2 Primary Antibody for ELISA, WB - ABIN543729
Browne, Finn, Proud: Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398. in The Journal of biological chemistry 2004
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Human Polyclonal PRKAA2 Primary Antibody for IF (p), IHC (p) - ABIN680458
Fu, Zhu, Dodson, Du: AMP-activated protein kinase stimulates Warburg-like glycolysis and activation of satellite cells during muscle regeneration. in The Journal of biological chemistry 2015
Show all 2 Pubmed References
Human Polyclonal PRKAA2 Primary Antibody for IF, IHC - ABIN6676477
Yang, He, Yao, Tan, Zhu, Li, Guo, Wei: Regulation of AMPK-related glycolipid metabolism imbalances redox homeostasis and inhibits anchorage independent growth in human breast cancer cells. in Redox biology 2018
Human Polyclonal PRKAA2 Primary Antibody for WB - ABIN6675675
Zheng, Zhou, Zhang, Thu, Xie, Lu, Pang, Xue, Xu, Chen, Chen, Li, Xu: Anhydroicaritin improves diet-induced obesity and hyperlipidemia and alleviates insulin resistance by suppressing SREBPs activation. in Biochemical pharmacology 2017
Human Polyclonal PRKAA2 Primary Antibody for ICC, IF - ABIN2855639
Zhang, Zhang, Zhou, Fu, Michal, Ji, Du, Davis, Jiang: Alternative polyadenylation drives genome-to-phenome information detours in the AMPKα1 and AMPKα2 knockout mice. in Scientific reports 2018
Human Polyclonal PRKAA2 Primary Antibody for ELISA, EIA - ABIN4280438
Dong, Zhang, Liang, Xie, Zhao, Asfa, Choi, Zou: Reduction of AMP-activated protein kinase alpha2 increases endoplasmic reticulum stress and atherosclerosis in vivo. in Circulation 2010
AMPKA2 activation increased the expression and nuclear localization of Twist1 which regulated epithelial-mesenchymal transition.
Mechanistically, AMP-activated protein kinase (AMPK)-mediated phosphorylation of BECN1 at Ser90/93/96 is required for BECN1-SLC7A11 complex formation and lipid peroxidation.
A double-negative feedback loop between Akt and AMPK controls the switch between matrix-attached and matrix-detached states needed to coordinate cell growth and survival during breast cancer metastasis.
It is an intracellular central metabolic sensor as well as a regulator, has been demonstrated to play significant roles in the contracting skeletal muscles, suggesting that AMPK should be one of the key molecules mediating metabolic effects during physical exercise.
PRKAA2 Polymorphisms in rs10789038 and rs2796498 are associated with the susceptibility to type 2 diabetes mellitus and diabetic nephropathy.
Lack of mitochondrial DNA impairs chemical hypoxia-induced autophagy in liver tumor cells through reactive oxygen species-AMPK-ULK1 signaling dysregulation independently of HIF-1A.
PRKAA deletion promoted mitochondrial fragmentation in vascular endothelial cells by inhibiting the autophagy-dependent degradation of DNM1L.
AMPK phosphorylates DNMT1, RBBP7, and HAT1 and increases interactions of DNMT1, RBBP7, and HAT1.
PGC-1alpha protein was higher after HIHVT than after SIT (p < 0.05). Moreover, the AMPKpTHR172/AMPK ratio increased at post after SIT (p < 0.05), whereas this effect was delayed after HIHVT as it increased after 3 h
TNF-alpha treatment of colonic rho(0) cells augmented IL-8 expression by 9-fold (P < 0.01) via NF-kappaB compared to TNF-alpha-treated control. Moreover, reduced mitochondrial function facilitated TNF-alpha-mediated NF-kappaB luciferase promoter activity as a result of lowered inhibitory IkappaBalpha (nuclear factor of kappa light polypeptide gene enhancer in B-cell inhibitor, alpha), leading to elevated NF-kappaB. ...
Results highlight the contribution of AMPKalpha2 as a mechanism for controlling bladder cancer growth by regulating proliferation through mTOR suppression and induction of p27 protein levels, thus indicating how AMPKalpha2 loss may contribute to tumorigenesis.
AMPK phosphorylation of cortactin followed by SIRT1 deacetylation modulates the interaction of cortactin and cortical-actin in response to shear stress. Functionally, this AMPK/SIRT1 coregulated cortactin-F-actin dynamics is required for endothelial nitric oxide synthase subcellular translocation/activation and is atheroprotective.
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.
inactivation of AMPKalpha2, but not AMPKalpha1, abrogates the tumor attenuation caused by UBE2O loss.
Our findings demonstrate that the AMPKalpha2 catalytic subunit in Kiss1 cells is dispensable for body weight and reproductive function in mice but is necessary for the reproductive adaptations to conditions of acute metabolic distress.
Binding of miR-27a to the 3'-UTR of the AMPKalpha2 gene was required to increase the sensitivity of breast cancer cells to metformin.
human cells were infected with lentiviruses expressing shRNA targeting both alpha1 and alpha2 AMPK subunits. AMPK activation inhibits Gli1-driven proliferation and that this effect is linked to Ser408 phosphorylation, which represents a key metabolic checkpoint for Hh signaling.
These data are in accordance with R6 binding directly to AMPKbeta2 when both proteins detach from the diminishing glycogen particle, which is simultaneous with increased AMPKbeta2 Thr-148 autophosphorylation.
p-AMPKalpha was associated with cervical carcinogenesis, and high expression of AMPKalpha2 was correlated with better disease-free survival in patients with early-stage cervical cancer
AMPK-alpha-2 binds to ER-alpha, as well as ER-beta.
AMPKalpha influences SERCA2a and phospholamban protein content in the sedentary and exercised heart
These results indicate that the AMPKalpha2 subunit in myeloid cells influences DNA methylation and thus protein expression and contributes to the development of atherosclerotic plaques.
miR-27b directly targets AMPK and inhibits AMPK expression. In cultured neural stem cells, miR-27b inhibitor improved proliferation and differentiation via the AMPK signaling pathway, but did not have an obvious effect on cell viability under oxygen and glucose deprivation conditions.
Phosphorylation of PINK1 by AMPKalpha2 was essential for efficient mitophagy to prevent the progression of heart failure.
Data show that sestrins (SESNs) are induced by AMPKalpha2 after exercise training, and SESNs, specifically SESN3, play a key role in exercise training-mediated glucose metabolism in skeletal muscle.
AMPKalpha2 regulates gene expressions including MCK, PGC-1alpha1 and PGC-1alpha4 and mitochondria-specific genes such as cytochrome c during the late stage of differentiation. Furthermore, the nuclear translocation of AMPKalpha2 is necessary for maintenance of PGC-1alpha1 mRNA during myogenesis.
AMPK alpha2 role in the mast cell activation and anaphylaxis.Sirt1 negatively regulates Fc epsilon RI-stimulated mast cell activation and anaphylaxis through two mutually regulated pathways involving AMP-activated protein kinase (AMPK) and protein tyrosine phosphatase 1B.AMPKalpha2 reciprocally activates Sirt1 in mast cells.
The authors found that the beta-adrenoceptor activation resulting from catecholamine release was mainly responsible for the changes of electrophysiology related to the absence of AMPKalpha2.
AMPK mediates the progress of atrophy during unloading and regrowth of atrophied muscles following reloading, but it does not influence the transition of myosin heavy chain isoforms.
Those findings provide new insight into the mechanisms responsible for AMPKalpha2-dependent regulation of GLUT4 transcription after exercise.
Thus, these findings suggest that AMPKalpha1 and AMPKalpha2 activity in chondrocytes is important in maintaining joint homeostasis and osteoarthritis development.
At molecular analysis, there was a time-dependent nuclear translocation of the active phosphorylated catalytic subunits AMPKalpha1/alpha2 and PGC-1alpha in young, but not in mature, mice after sepsis.
Study indicate that the alpha 2 and alpha 1 subunits of AMPK have several functional differences, with alpha 2 conferring stronger osteogenic potential and a weaker ability to induce osteoblasts-associated osteoclastogenesis in MC3T3-E1 cells as well as conferring a lower adipogenic potential to 3T3-L1 cells.
activation of AMPK at early stage of adipogenesis is involved in the anti-adipogenesis effect of Red Pepper Seed extract.
data suggest that AMPK is an intermediate effector in endocannabinoid-mediated exercise-induced antinociception.
The rs2746342 polymorphism is significantly associated with susceptibility to type 2 diabetes mellitus (T2DM) and seems to interact with the rs2143754 polymorphism in the modulation of fasting plasma glucose (FPG) in the Han Chinese population.
AMPKalpha2 activation prevents cardiac hypertrophy predominantly by inhibiting O-GlcNAcylation.
Ampk is required for exercise-induced mitophagy in muscle.
results indicate that liver AMPKalpha1alpha2 is required for maintaining glucose homeostasis during an acute bout of exercise.
Single SNP and haplotype analyses revealed weak associations between the PRKAA2 genotypes and loin muscle area in the investigated populations.
Endometrial inflammatory responses to lipopolysaccharide were also reduced by small molecules that activate or inhibit the intracellular sensor of energy, AMP-activated protein kinase (AMPK).
The investigation of PRKAA2 genetic polymorphisms in three Chinese indigenous bovine breeds [Qinchuan (n = 328), Nanyang (n = 278), Jiaxian (n = 148)] and yak (n = 57), is reported.
These data show that the AMPK activator AICAR is inhibitory to nuclear maturation in bovine oocytes due to activation of AMPK [AMP-activated protein kinase alpha 1 subunit].
The protein encoded by this gene is a catalytic 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. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.
5'-AMP-activated protein kinase catalytic subunit alpha-2
, 5'-AMP-activated protein kinase, catalytic alpha-2 chain
, ACACA kinase
, AMPK subunit alpha-2
, AMPK-alpha-2 chain
, HMGCR kinase
, acetyl-CoA carboxylase kinase
, hydroxymethylglutaryl-CoA reductase kinase
, AMP-activated protein kinase
, AMPK alpha-2 chain
, AMP-activated protein kinase alpha-2 variant B
, AMP-activated protein kinase alpha 2
, protein kinase AMP-activated alpha 2 catalytic subunit
, SNF1-like protein AMPK
, 5'-AMP-activated protein kinase alpha-2 catalytic subunit
, AMP-activated protein kinase alpha 2 catalytic subunit
, protein kinase, AMP-activated, alpha 2 catalytic subunit
, AMPK-activated protein kinase alpha-2 subunit