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ADH4 encodes class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Additionally we are shipping Alcohol Dehydrogenase 4 (Class II), pi Polypeptide Antibodies (58) and Alcohol Dehydrogenase 4 (Class II), pi Polypeptide Proteins (8) and many more products for this protein.
Showing 9 out of 9 products:
this current study provides substantial evidence that genetic polymorphisms of rs3805322 in the ADH4 gene may be associated with an increased risk of developing ESCC in two Chinese Han populations.
This study confirmed the genetic heterogeneity of cluster headache, suggesting that mutations in the ADH4 gene might be related to cluster headache in a subset of cases.
The serum expression of ADH4 protein correlates with the progression of esophageal cancer.
common ADH (show AVP ELISA Kits) variants conferred risk for both schizophrenia in African-Americans and autism in European-Americans.
expression levels of ADH4 mRNA and protein have found to be markedly reduced in hepatocellular carcinoma (HCC (show FAM126A ELISA Kits)) tissues and significantly associated with survival.
data suggest that ADH4 intronic variants play a role in alcohol dependence susceptibility in Italian populations
Variants in the ADH1B and ADH4 genes may be protective against the development of some symptoms associated with alcohol dependence.
Our results suggest that the analysed polymorphisms ofANKK1 and ADH4 can play an important part in the pathogenesis of alcohol abuse
the high catalytic activity of human alcohol dehydrogenase 4 studied with horse liver ADH1E
This study confirms the significant relationship of ADH4 variants with AD and related phenotypes.
This study demonistrated that adh1/adh4 knockout mice as possible rodent models for presymptomatic Parkinson's disease.
The results suggested that lack of Adh4 gene activity induces changes in the function of the dopamine system, findings which are compatible with a role of loss-of-function mutations in ADH4 as possible risk factors for parkinson disease.
Distinct retinoid metabolic functions for alcohol dehydrogenase genes Adh1 and Adh4 in protection against vitamin A toxicity or deficiency revealed in double null mutant mice
Studies of kinetic properties of mouse ADH2 in new variants with substitutions at position 47 find that the pK values are not lowered by Pro47 to His substitution, suggesting that His47 does not act as a catalytic base in deprotonation of the zinc ligand.
Adh4 metabolizes the omega-oxidation of 20-HETE in cerebral microvascular smooth muscle and endothelium.
Cellular expression of Adh4 in the GI tract was studied.
The metabolism of all-trans- and 9-cis (show RDH11 ELISA Kits)-retinol/ retinaldehyde has been investigated with focus on the activities of human, mouse and rat alcohol dehydrogenase 2 (ADH2 (show ADH1B ELISA Kits)), an intriguing enzyme with apparently different functions in human and rodents.
This gene encodes class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class II alcohol dehydrogenase is a homodimer composed of 2 pi subunits. It exhibits a high activity for oxidation of long-chain aliphatic alcohols and aromatic alcohols and is less sensitive to pyrazole. This gene is localized to chromosome 4 in the cluster of alcohol dehydrogenase genes.
alcohol dehydrogenase Adh4
, alcohol dehydrogenase 4
, alcohol dehydrogenase class II pi chain
, aldehyde reductase
, alcohol dehydrogenase II
, alcohol dehydrogenase class II
, class II alcohol dehydrogenase, pi subunit
, class II type ADH