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anti-Rat (Rattus) HADH Antibodies:
anti-Human HADH Antibodies:
anti-Mouse (Murine) HADH Antibodies:
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Human Monoclonal HADH Primary Antibody for IF, IHC (p) - ABIN561223
Tönjes, Barbus, Park, Wang, Schlotter, Lindroth, Pleier, Bai, Karra, Piro, Felsberg, Addington, Lemke, Weibrecht, Hovestadt, Rolli, Campos, Turcan, Sturm, Witt, Chan, Herold-Mende, Kemkemer, König et al.: BCAT1 promotes cell proliferation through amino acid catabolism in gliomas carrying wild-type IDH1. ... in Nature medicine 2013
Show all 3 Pubmed References
Dog (Canine) Polyclonal HADH Primary Antibody for ELISA, WB - ABIN548051
Molven, Matre, Duran, Wanders, Rishaug, Njølstad, Jellum, Søvik: Familial hyperinsulinemic hypoglycemia caused by a defect in the SCHAD enzyme of mitochondrial fatty acid oxidation. in Diabetes 2003
The most frequently seen mutations in Turkish patients with congenital hyperinsulinism (CHI) were ATP binding cassette subfamily C member 8 (ABCC8) gene, followed by 3-hydroxyacyl CoA dehydrogenase (HADH) and kcnj11 channel (KCNJ11) genes.
Paretic muscle in hemiparetic stroke survivors had lower HAD concentration.
We present clinical and laboratory findings together with the long-term clinical course of a case with a deep intronic HADH splicing mutation (c.636+471G>T) causing neonatal-onset hyperinsulinemic hypoglycemia with mild progression
in a cohort of hyperinsulinemic hypoglycemia patients from Isfahan, Iran, 78% were noted to have disease-causing mutations: 48% had HADH mutations and 26% had ABCC8 mutations.
Next-generation sequencing reveals deep intronic cryptic ABCC8 and HADH splicing founder mutations causing hyperinsulinism by pseudoexon activation.
Loss of function mutations in 3-Hydroxyacyl-CoA Dehydrogenase (HADH) cause leucine sensitive hyperinsulinaemic hypoglycaemia.
Clinical, biochemical and molecular findings of four new Caucasian patients with HADH deficiency.
We recommend that HADH sequence analysis is considered in all patients with diazoxide-responsive hyperinsulinemic hypoglycemia when recessive inheritance is suspected
Congenital hyperinsulinism due to mutations in HNF4A and HADH.
SCHAD deficiency can result in persistent hyperinsulinemic hypoglycemia of infancy
Unlikely that variation in HADHSC plays a major role in the pathogenesis of type 2 diabetes in the examined cohorts.
This case indicates that mutations of the HADH gene should be sought in hyperinsulinemic patients in whom diffuse form of hyperinsulinemic hypoglycemia.
To investigate its function in this catalytic dyad, Glu(170) was replaced with glutamine (E170Q), and the mutant enzyme was characterized. Substrate and cofactor binding were unaffected by the mutation; E170Q exhibited diminished catalytic activity
Patients with the G1528C mutation of 3-hyroxyacyl-CoA dehydrogenase exhibit hepatomegaly and steatosis of the liver, as well as accumulation of fat in the myocardium, renal tubules, and skeletal muscle
A physical association between short-chain 3-hydroxyacyl-coenzyme A dehydrogenase and important components of other key metabolic pathways. Most of the interactions were with enzymes in mitochondrial pathways.
SCHAD is involved in thermogenesis, in the maintenance of body weight, and in the regulation of nutrient-stimulated insulin secretion
SCHAD deficiency causes hyperinsulinism by activation of GDH via loss of inhibitory regulation of GDH by SCHAD.
Results demonstrate that L-3-hydroxyacyl-CoA dehydrogenase type II (HADH II/ABAD) modulates 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine neurotoxicity and suggests that mimetics may provide protective benefit in the treatment of Parkinson disease.
SCHAD regulates insulin secretion through a KATP channel-independent mechanism.
This gene is a member of the 3-hydroxyacyl-CoA dehydrogenase gene family. The encoded protein functions in the mitochondrial matrix to catalyze the oxidation of straight-chain 3-hydroxyacyl-CoAs as part of the beta-oxidation pathway. Its enzymatic activity is highest with medium-chain-length fatty acids. Mutations in this gene cause one form of familial hyperinsulinemic hypoglycemia. The human genome contains a related pseudogene of this gene on chromosome 15.
, L-3-hydroxyacyl-CoA dehydrogenase
, hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
, medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase
, medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase
, short chain 3-hydroxyacyl-CoA dehydrogenase
, short-chain 3-hydroxyacyl-CoA dehydrogenase
, L-3-hydroxyacyl-Coenzyme A dehydrogenase
, L-3-hydroxyacyl-Coenzyme A dehydrogenase, short chain
, hydroxyacyl-Coenzyme A dehydrogenase
, hydroxylacyl-Coenzyme A dehydrogenase short chain
, hydroxylacyl-Coenzyme A dehydrogenase, short chain
, hydroxylacyl-Coenzyme A dehydrogenase-dehydrogenase
, 3-hydroxyacyl-CoA dehydrogenase (short-chain)
, Short chain 3-hydroxyacyl-CoA dehydrogenase
, short chain 3-hydroxyacyl-coa dehydrogenase