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anti-Human ETFDH Antibodies:
anti-Mouse (Murine) ETFDH Antibodies:
anti-Rat (Rattus) ETFDH Antibodies:
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Human Polyclonal ETFDH Primary Antibody for WB - ABIN6679927
Qiu, Liu, Cheng, Wang, Jing, Pei, Zhao, Wang, Guo, Zhang: Impaired Autophagy and Defective T Cell Homeostasis in Mice with T Cell-Specific Deletion of Receptor for Activated C Kinase 1. in Frontiers in immunology 2017
Human Polyclonal ETFDH Primary Antibody for ELISA, WB - ABIN4309655
Illig, Gieger, Zhai, Römisch-Margl, Wang-Sattler, Prehn, Altmaier, Kastenmüller, Kato, Mewes, Meitinger, de Angelis, Kronenberg, Soranzo, Wichmann, Spector, Adamski, Suhre: A genome-wide perspective of genetic variation in human metabolism. in Nature genetics 2010
Multiple acyl-CoA dehydrogenase deficiency is cause by electron transfer flavoprotein ubiquinone oxidoreductase mutation at heterozygotes with c.1354A>G (p.Arg452Gly) and exon 7-8 deletion for Patient 1, and with c.831+3A>C and exon 1-7 deletion for Patient 2.
This case report extends the spectrum of ETFDH mutations in multiple acyl-CoA dehydrogenase deficiency (MADD), providing further evidence that patients presenting at least one missense mutation in the FAD-binding domain may respond to either carnitine or riboflavin treatment, due to the recovery of some enzymatic activity.
Neurite shortening and impairment in neurite growth was caused by a mutation in ETFDH.
This study identified three novel compound heterozygous mutations of ETFDH gene in patients with late-onset multiple acyl-CoA dehydrogenase deficiency, and discussed the significant clinical heterogeneity among patients with similar genotype.
ETFDH mutation is the causative gene in patients with adult-onset multiple acyl-CoA dehydrogenase deficiency with severe sensory neuropathy.
Mtation c.250G>A and mutation c.353G>T in the ETFDH gene are associate with multiple aeyl-CoA dehydrogenase deficiency with severe fatty liver.
identified 61 ETFDH mutations, including 31 novel mutations, which were widely distributed within the coding sequence
Mutations in SLC22A5 and ETFDH are associated with riboflavin responsive-multiple acyl-CoA dehydrogenase deficiency.
Results show that a predicted benign ETFDH missense variationc.158A>G in exon 2 causes exon skipping and degradation of ETFDH protein in patient samples.
Case Report: ETF dehydrogenase mutations resulting in mild glutaric aciduria type II and complex II-III deficiency in liver and muscle.
folding defects in the variant ETF-QO proteins and multiple acyl-CoA dehydrogenation deficiency
a significant reduced expression of ETFDH was identified in the muscle of ETFDH-deficient patients; ETFDH deficiency is a major cause of riboflavin-responsive MADD in southern China, and c.250G>A is an important mutation
High frequency of ETFDH c.250G>A mutation in Taiwanese patients with late-onset lipid storage myopathy
3 known (c.250G>A, c380T>A, c.524G>T) and 1 novel (c.1831G>A) ETFDH mutation were detected by high resolution melting analysis. The carrier frequency of the hotspot mutation, c.250G>A, in the Taiwanese population was found to be 1:125.
lipid storage myopathy caused by ETFDH gene mutations.
expression from a baculovirus vector and kinetic and spectral characteristics
Mutations are identified by molecular analysis of 20 ETF:QO-deficient patients. Twenty-one different disease-causing mutations were identified on 36 of the 40 chromosomes.
patients had autosomal recessive mutations in ETFDH, suggesting ETFDH deficiency leads to a secondary CoQ10 deficiency; results indicate that the late-onset form of glutaric aciduria type II & the myopathic form of CoQ10 deficiency are allelic diseases
study identified ETFDH mutations in all members of a large series of patients with riboflavin-responsive multiple acyl-CoA dehydrogenation deficiency
We performed mutation analysis in four Taiwanese MADD patients. Three novel ETFDH mutations were identified in four patients and all harbored the p.A84T mutation
Data indicate that the iron-sulfur cluster of electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) is the electron acceptor for electron transfer flavoprotein.
Studies indicate that ETF-QO to be a monotopic membrane protein with the cofactors, FAD and a [4Fe-4S](+1+2) cluster, suggesting that it is the flavin that serves as the immediate reductant of ubiquinone.
Electron-transferring-flavoprotein dehydrogenase in the inner mitochondrial membrane accepts electrons from electron-transfer flavoprotein which is located in the mitochondrial matrix and reduces ubiquinone in the mitochondrial membrane. The protein is synthesized as a 67-kDa precursor which is targeted to mitochondria and processed in a single step to a 64-kDa mature form located in the mitochondrial membrane. Deficiency in electron-transferring-flavoprotein dehydrogenase have been demonstrated in some patients with type II glutaricacidemia.
, ETF-ubiquinone oxidoreductase
, electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
, electron-transferring-flavoprotein dehydrogenase
, electron transferring flavoprotein dehydrogenase
, Electron-transferring-flavoprotein dehydrogenase
, Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
, LOW QUALITY PROTEIN: electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial