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HADH is a member of the 3-hydroxyacyl-CoA dehydrogenase gene family. Additionally we are shipping HADH Proteins (11) and HADH Kits (5) and many more products for this protein.
Showing 10 out of 132 products:
Human Monoclonal HADH Primary Antibody for WB - ABIN395923
Kalsi, Kuo, Aliev, Alexander, McMichael, Patterson, Walsh, Zhao, Schuckit, Nurnberger, Edenberg, Kramer, Hesselbrock, Tischfield, Vladimirov, Prescott, Dick, Kendler, Riley: A systematic gene-based screen of chr4q22-q32 identifies association of a novel susceptibility gene, DKK2, with the quantitative trait of alcohol dependence symptom counts. in Human molecular genetics 2010
Show all 5 references for ABIN395923
Human Monoclonal HADH Primary Antibody for IF, WB - ABIN396238
Di Candia, Gessi, Pepe, Sogno Valin, Mangano, Chiumello, Gianolli, Proverbio, Mora: Identification of a diffuse form of hyperinsulinemic hypoglycemia by 18-fluoro-L-3,4 dihydroxyphenylalanine positron emission tomography/CT in a patient carrying a novel mutation of the HADH gene. in European journal of endocrinology / European Federation of Endocrine Societies 2009
Show all 5 references for ABIN396238
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 references for ABIN561223
Dog (Canine) Polyclonal HADH Primary Antibody for WB - ABIN374901
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
Chicken Polyclonal HADH Primary Antibody for WB - ABIN2785872
van Hove, Hansen, Dekker, Reiling, Nijpels, Jørgensen, Borch-Johnsen, Hamid, Heine, Pedersen, Maassen, t Hart: The HADHSC gene encoding short-chain L-3-hydroxyacyl-CoA dehydrogenase (SCHAD) and type 2 diabetes susceptibility: the DAMAGE study. in Diabetes 2006
We present clinical and laboratory findings together with the long-term clinical course of a case with a deep intronic HADH (show HADHA Antibodies) 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 (show HADHA Antibodies) mutations and 26% had ABCC8 (show ABCC8 Antibodies) mutations.
Next-generation sequencing reveals deep intronic cryptic ABCC8 (show ABCC8 Antibodies) and HADH (show HADHA Antibodies) 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 (show HADHA Antibodies) deficiency.
We recommend that HADH (show HADHA Antibodies) sequence analysis is considered in all patients with diazoxide-responsive hyperinsulinemic hypoglycemia when recessive inheritance is suspected
Congenital hyperinsulinism due to mutations in HNF4A (show HNF4A Antibodies) and HADH (show HADHA Antibodies).
SCHAD (show HSD17B10 Antibodies) 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 (show HADHA Antibodies) gene should be sought in hyperinsulinemic patients in whom diffuse form of hyperinsulinemic hypoglycemia.
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 (show HSD17B10 Antibodies) is involved in thermogenesis, in the maintenance of body weight, and in the regulation of nutrient-stimulated insulin (show INS Antibodies) secretion
SCHAD (show HSD17B10 Antibodies) deficiency causes hyperinsulinism by activation of GDH (show UGDH Antibodies) via loss of inhibitory regulation of GDH (show UGDH Antibodies) by SCHAD (show HSD17B10 Antibodies).
Results demonstrate that L-3-hydroxyacyl-CoA dehydrogenase type II (show HSD17B10 Antibodies) (HADH (show HSD17B10 Antibodies) II/ABAD (show HSD17B10 Antibodies)) 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 (show HSD17B10 Antibodies) regulates insulin (show INS Antibodies) 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.
hydroxyacyl-Coenzyme A dehydrogenase
, L-3-hydroxyacyl-Coenzyme A dehydrogenase
, L-3-hydroxyacyl-Coenzyme A dehydrogenase, short chain
, hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
, 3-hydroxyacyl-CoA dehydrogenase (short-chain)
, Short chain 3-hydroxyacyl-CoA dehydrogenase
, short chain 3-hydroxyacyl-coa dehydrogenase
, medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase
, short-chain 3-hydroxyacyl-CoA dehydrogenase
, hydroxylacyl-Coenzyme A dehydrogenase short chain
, hydroxylacyl-Coenzyme A dehydrogenase, short chain
, medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase
, short chain 3-hydroxyacyl-CoA dehydrogenase
, L-3-hydroxyacyl-CoA dehydrogenase
, hydroxylacyl-Coenzyme A dehydrogenase-dehydrogenase