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anti-Human CPT2 Antibodies:
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Human Polyclonal CPT2 Primary Antibody for ELISA, WB - ABIN545297
Britton, Schultz, Zhang, Esser, Foster, McGarry: Human liver mitochondrial carnitine palmitoyltransferase I: characterization of its cDNA and chromosomal localization and partial analysis of the gene. in Proceedings of the National Academy of Sciences of the United States of America 1995
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Human Polyclonal CPT2 Primary Antibody for ELISA, WB - ABIN545298
Deschauer, Wieser, Schröder, Zierz: A novel nonsense mutation (515del4) in muscle carnitine palmitoyltransferase II deficiency. in Molecular genetics and metabolism 2002
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Human Polyclonal CPT2 Primary Antibody for ELISA, WB - ABIN4300344
Isackson, Bennett, Lichter-Konecki, Willis, Nyhan, Sutton, Tein, Vladutiu: CPT2 gene mutations resulting in lethal neonatal or severe infantile carnitine palmitoyltransferase II deficiency. in Molecular genetics and metabolism 2008
Human Polyclonal CPT2 Primary Antibody for WB - ABIN947728
Console, Giangregorio, Indiveri, Tonazzi: Carnitine/acylcarnitine translocase and carnitine palmitoyltransferase 2 form a complex in the inner mitochondrial membrane. in Molecular and cellular biochemistry 2014
Lack of activation of the S113L variant of carnitine palmitoyltransfersase II by cardiolipin.
The results show that AMPK activation by GSK773 evokes the slow, oxidative myogenic program and triggers beneficial phenotypic adaptations in FAO-deficient myotubes. Thus, GSK773 might have therapeutic potential for correction of CPT2 deficiency
To the best of our knowledge, this is the first report of the coexistence of VHL disease and CPT2 deficiency in the same individual. Based on findings from animal models, the case illustrates that mutations in the VHL gene might protect against renal damage caused by CPT2 gene mutations.
this study shows that upregulation of the citrate pathway and down-regulation of carnitine/acylcarnitine carrier gene in cells from children with Down syndrome
The clinical presentation of patients with muscle carnitine palmitoyltransferase II deficiency is discussed in this review in line with enzymatic features. The thermolability of the mutant enzyme might explain why symptoms in muscle CPT II deficiency mainly occur during prolonged exercise, infections and exposure to cold. [review]
Variations in AMPD1, CPT2, and PGYM genes are not associated with the onset, susceptibility, or severity of chronic fatigue syndrome.
polymorphism may be associated with severity of EV71 infection
CPT2 is active inside the mitochondrial matrix to recover acyl-CoA from a process generally known as the carnitine shuttle. This protein is expressed in a constitutive way in all cells and tissues.
CPT II deficiency induces an energy crisis of the fatty acid metabolic pathway.
L-carnitine deficiency participates in the pathogenesis of endometrial cancer by means of a mechanism which is unrelated with obesity and increased amount of fat in human body.
The rs2229291 and rs1799821 variants in CPT II gene might be one of the predisposing factors of acute encephalitis.
The F352C CPT2 variant might be a genetic risk factor for sudden unexpected death in infancy
The data indicate that within the muscle form of CPT II deficiency, the various genotypes have only marginal influence on the clinical and biochemical phenotype.
The present study shows that screening for second mutations in patients that are heterozygote for the common p.S113L is justified although rare symptomatic heterozygotes.
The homozygous genotype (AA) of CPT2 variant V368I had significantly less blood carnitine in acute myocardial infarction patients.
Allelic and phenotypic heterogeneity in 49 Italian patients with the muscle form of CPT-II deficiency
CPT2 and CACT are crucial for mitochondrial acylcarnitine formation and export to the extracellular fluids in mitochondrial fatty acid beta-oxidation disorders.
the thermolabile F352C CPT II variant, found only in Japanese, might be one of the predisposing factors to trigger the pathomechanism of acute encephalopathy in the Japanese population
A homozygous mutation (c.534_558del25bpinsT) of CPT2 in a case of neonatal CPT II deficiency associated with Dandy-Walker syndrome and sudden death at 13 days of life.
Data demonstrated the thermolabile CPT-II variants in demonstrated the thermolabile CPT-II variants in patients with viral infection-associated encephalopathy in Chinese population.
Cpt2 is obligate enzyme in long-chain fatty acid (FA) oxidation; cardiac hypertrophy is linked to impaired FA oxidation. Data (including data from studies using transgenic/knockout mice) suggest that deficiency of Cpt2 in cardiac muscle leads to cardiac hypertrophy/dysfunction with eventual lethality without cardiac fibrosis; mTORC1 is activated in Cpt2(-/-) heart, but inhibition of mTORC1 does not prevent hypertrophy.
Mice acclimatized to thermoneutrality revealed that Cpt2A-null interscapular brown adipose tissue failed to induce the expression of thermogenic genes such as Ucp1 and Pgc1a.
Consistent with the known requirement for CPT2 in fatty acid oxidation, macrophages lacking CPT2 were unable to achieve b-oxidation of fatty acids yet still seemed to fully polarize toward an M2 state after stimulation with IL-4 in vitro and in vivo.
Cpt2 transcripts decrease following fertilization to undetectable levels and are present again later at the morula stage
It was conclude that suppression of CPT activity by positive energy balance appears to be specific for the liver in mid-lactating dairy cows.
The protein encoded by this gene is a nuclear protein which is transported to the mitochondrial inner membrane. Together with carnitine palmitoyltransferase I, the encoded protein oxidizes long-chain fatty acids in the mitochondria. Defects in this gene are associated with mitochondrial long-chain fatty-acid (LCFA) oxidation disorders.
carnitine O-palmitoyltransferase 2, mitochondrial
, carnitine palmitoyltransferase II
, carnitine palmitoyltransferase 2
, carnitine O-palmitoyltransferase
, carnitine O-palmitoyltransferase 2, mitochondrial-like
, CPT II
, mitochondrial carnitine palmitoyltransferase II