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The protein encoded by ACADVL is targeted to the inner mitochondrial membrane where it catalyzes the first step of the mitochondrial fatty acid beta-oxidation pathway. Additionally we are shipping ACADVL Proteins (13) and many more products for this protein.
Showing 10 out of 66 products:
Human Monoclonal ACADVL Primary Antibody for WB - ABIN396579
Pan, Chen, Pan, Wang, Han, Zheng, Wang, Li, Qu, Shao: Differential gene expression identified in Uigur women cervical squamous cell carcinoma by suppression subtractive hybridization. in Neoplasma 2010
Show all 5 references for ABIN396579
Cow (Bovine) Polyclonal ACADVL Primary Antibody for WB - ABIN2785735
Soon, Libe, Benn, Gill, Shaw, Sywak, Groussin, Bertagna, Gicquel, Bertherat, McDonald, Sidhu, Robinson: Loss of heterozygosity of 17p13, with possible involvement of ACADVL and ALOX15B, in the pathogenesis of adrenocortical tumors. in Annals of surgery 2007
Show all 2 references for ABIN2785735
Human Monoclonal ACADVL Primary Antibody for IHC (p), ELISA - ABIN559746
De Pauw, Demine, Tejerina, Dieu, Delaive, Kel, Renard, Raes, Arnould: Mild mitochondrial uncoupling does not affect mitochondrial biogenesis but downregulates pyruvate carboxylase in adipocytes: role for triglyceride content reduction. in American journal of physiology. Endocrinology and metabolism 2012
Show all 2 references for ABIN559746
Human Polyclonal ACADVL Primary Antibody for EIA, WB - ABIN615945
Gobin-Limballe, Djouadi, Aubey, Olpin, Andresen, Yamaguchi, Mandel, Fukao, Ruiter, Wanders, McAndrew, Kim, Bastin: Genetic basis for correction of very-long-chain acyl-coenzyme A dehydrogenase deficiency by bezafibrate in patient fibroblasts: toward a genotype-based therapy. in American journal of human genetics 2007
11 mutations in ACADVL gene in 7 patients, 7 reported (p.S22X, p.W427X, p.A213T, p.G222R, p.R450H, c.296-297delCA, c.1605+1G>T), 4 novel (p.S72F, p.Q100X, p.M437T, p.D466Y). p.R450H and p.D466Y (14.28%, 2/14 alleles) mutations identified in 2 alleles.
Case Report: missense mutation within the ACADVL gene responsible for very-long-chain acyl-CoA dehydrogenase deficiency and sudden infant death.
These results emphasize the importance of functional investigation of abnormal NBS (show NBN Antibodies) or clinical testing suggestive but not diagnostic of very-long-chain acyl-CoA dehydrogenase .
These findings support the importance of considering that mutations may be present in the ACADVL gene when a significant partial deficiency is found in CPTII (show CPT2 Antibodies) activity, but no mutations in the CPT2 (show CPT2 Antibodies) gene can be identified.
Identification of 2 VLCAD mutations leads to precautions in the management of the children with VLCAD deficiency.
The expressions of LCHAD (show HADHA Antibodies) gene and protein are remarkably reduced in early onset severe preeclampsia and HELLP syndrome.
Analyzed potential rhabdomyolysis-susceptibility genes (RYR 1 (show RYR1 Antibodies), CPT II (show CPT2 Antibodies), VLCAD and CYP (show PPIG Antibodies) 2D6) from autopsy samples of methamphetamine abusers; no obvious relationship between the genetic mutations observed in this study and rhabdomyolysis was seen.
Down regulation of ACADVL is associated with cervical squamous cell carcinoma.
Missense mutations in Very-Long-Chain Acyl-CoA Dehydrogenase is associated with inborn errors of lipid metabolism.
This study confirms that VLCAD deficiency, although being less frequent than CPT II (show CPT2 Antibodies) deficiency, should be systematically considered in the differential diagnosis of exercise-induced rhabdomyolysis.
Bovine ACADVL gene had a significant effect on chest width (P<0.05), chest depth (P<0.05), and hip width (P<0.05) in the Qinchuan breed.
observed strong upregulation of peroxisomal beta-oxidation in VLCAD(-/-) mice
SIRT3 (show SIRT3 Antibodies) and SIRT5 (show SIRT5 Antibodies) regulate the enzyme activity and cardiolipin binding of very long-chain acyl-CoA dehydrogenase
Studies conducted with permeabilized mitochondria and different chain length acyl-CoA (show GNPAT Antibodies) derivatives suggest that VLCAD is also a source of reactive oxygen species production in mitochondria of high fat diet animals.
We demonstrate here that both dietary interventions with respect to the fat content of the diet reverse endogenous compensatory mechanisms in muscle that have evolved in VLCAD(-/-) mice resulting in pronounced energy deficiency
VLCAD(-/-) mice develop tissue-specific strategies to compensate deficiency of VLCAD either by induction of other mitochondrial acyl-CoA (show GNPAT Antibodies) dehydrogenases or by enhancement of glucose oxidation.
Report a longer QTc interval and lipid alterations in VLCAD null mice.
Four VLCAD-/- deficient mice died unexpectedly on the treadmill during the early stages of training. The VLCAD-/- deficient mice that survived adapted to the aerobic interval training similarly to the non-deficient mice.
Medium-chain triglycerides impair lipid metabolism and induce hepatic steatosis in very long-chain acyl-CoA dehydrogenase (VLCAD)-deficient mice
Data show that in VLCAD knockout mice fed a long-chain triglyceride diet, fasting results in accumulation of liver lipids, hepatopathy and upregulation of peroxisomal and microsomal oxidation pathways as well as antioxidant enzyme activities and TBARS.
medium-chain triglyceride application prevents acylcarnitine accumulation in skeletal muscle from very-long-chain acyl-CoA-dehydrogenase-deficient mice
The protein encoded by this gene is targeted to the inner mitochondrial membrane where it catalyzes the first step of the mitochondrial fatty acid beta-oxidation pathway. This acyl-Coenzyme A dehydrogenase is specific to long-chain and very-long-chain fatty acids. A deficiency in this gene product reduces myocardial fatty acid beta-oxidation and is associated with cardiomyopathy. Alternative splicing results in multiple transcript variants encoding different isoforms.
acyl-Coenzyme A dehydrogenase, very long chain
, very long-chain specific acyl-CoA dehydrogenase, mitochondrial
, acyl-coenzyme A dehydrogenase, very long chain
, VLCAD very-long-chain acyl-CoA dehydrogenase
, Very long chain Acyl-Coa dehydrogenase