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Validated All-in-One™ qPCR Primer for PRKAA2(NM_006252.3) Search again
Product ID:
HQP014541
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
AMPK, AMPK2, AMPKa2, PRKAA
Gene Description:
protein kinase AMP-activated catalytic subunit alpha 2
Target Gene Accession:
NM_006252.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
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.
Gene References into function
- Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase.
- Role of AMPK in tolerance to glucose starvation in cell lines
- AMPK signaling is not a key regulatory system of muscle substrate combustion during prolonged exercise and marked activation of AMPK via phosphorylation is not sufficient to maintain an elevated ACCbeta Ser(221) phosphorylation during prolonged exercise
- Regulation of channel gating by AMP-activated protein kinase modulates cystic fibrosis transmembrane conductance regulator activity in lung submucosal cells.
- Overexpression of mutant AMPK-alpha1 enhanced forskolin-stimulated I short-circuit currents, consistent with dominant-negative reduction in inhibition of CFTR by endogenous AMPK.
- results suggest that nuclear translocation of 5' AMP-activated protein kinase might mediate the effects of exercise on skeletal muscle gene and protein expression
- endothelial AMPK signaling may be a critical determinant of blood vessel recruitment to tissues that are subjected to ischemic stress.
- LKB1 kinase, which is associated with Peutz-Jeghers cancer-susceptibility syndrome, phosphorylates and activates AMPK in vitro.
- Acetyl-CoA carboxylase beta phosphorylation is especially sensitive to exercise and tightly coupled to AMPK signaling and that AMPK activation does not depend on AMPK kinase activation during exercise.
- This study demonstrates that protein content and basal AMPK activity in human skeletal muscle are highly susceptible to endurance exercise training.
- AMPK and eEF2 kinase may provide a key link between cellular energy status and the inhibition of protein synthesis, a major consumer of metabolic energy
- AMPK is a major regulator of skeletal muscle HSL activity that can override beta-adrenergic stimulation
- AMPK is a novel and critical component of HIF-1 regulation, implying its involvement in vanadate-induced prostate carcinogenesis
- Results indicate that AMP-activated protein kinase (AMPK)alpha negatively regulates acetyl-CoA carboxylase activity and hepatic lipid content.
- AMPK has a role in the phenobarbital induction of CYP2B gene expression
- AMPK has a major role in the post-transcriptional regulation of VEGF and a potential role in tumor angiogenesis
- Co-immunoprecipitation and binding assay data from both cell types show that the H1/A (but not H2/B) isoform of NDPK is associated with AMPK complexes containing the alpha1 (but not alpha2) catalytic subunit.
- There is a significant basal activity and phosphorylation of AMPK in LKB1-deficient cells that can be stimulated by Ca2+ ionophores, and studies using the CaMKK inhibitor STO-609 and isoform-specific siRNAs show that CaMKKbeta is required for this effect
- Overexpression of CaMKKbeta in mammalian cells increases AMPK activity, whereas pharmacological inhibition of CaMKK, or downregulation of CaMKKbeta using RNA interference, almost completely abolishes AMPK activation
- causes inappropriate AMP kinase activation, which leads to glycogen accumulation and heart conduction system disease when transfected into mice
- data suggest that moderate endurance exercise promotes glucose transport, GLUT4 expression, and insulin sensitivity in skeletal muscle at least partially via activation of the alpha2 isoform of AMPK
- These data suggest that prolonged hypoxia promotes the expression and functional activation of AMPKalpha2 and VEGF production in glioma cell lines and glioblastoma multiform tumors, thus contributing to tumor survival and angiogenesis in gliomas.
- PRKAA2 gene influences insulin resistance and susceptibility to type 2 diabetes in the Japanese population.
- Oral glucose ingestion attenuates the exercise-induced activation of alpha2-AMPK, bringing further support for a fuel-sensing role of AMPK in skeletal muscle.
- Findings indicate that AMPK activation in skeletal muscle during exercise is not sensitive to changes in plasma glucose levels in the normal range.
- AA454543 may have a role in progression of hepatocellular carcinoma after partial hepatectomy
- AMPK has a central role in stimulus-response coupling by hypoxia
- genetic variants of LKB1-AMPK-TORC2 pathway components may exert a weak influence on the occurrence of type 2 diabetes in Japanese
- alpha2 But not alpha1 AMP-activated protein kinase mediates oxidative stress-induced inhibition of retinal pigment epithelium cell phagocytosis of photoreceptor outer segments
- AMPK alpha2 activity, AMPK alpha2 Thr172 phosphorylation, and ACC-beta Ser222 phosphorylation were increased immediately after exercise. These increases had all returned to basal levels at 3 and 24 h after exercise.
- Results demonstrate that AMPK-alpha1 and AMPK-alpha2 activity and fuel selection in skeletal muscle in response to exercise can be manipulated by diet and/or the interactive effects of diet and exercise training.
- A novel AMPK-mediated regulatory pathway that regulates PGC-1alpha gene expression.
- The phosphorylation of GFAT1 at Ser243 by AMPK has an important role in the regulation of the GFAT1 enzymatic activity.