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Validated All-in-One™ qPCR Primer for ADH5(NM_000671.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
This gene encodes a member of the alcohol dehydrogenase family. Members of this family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. The encoded protein forms a homodimer. It has virtually no activity for ethanol oxidation, but exhibits high activity for oxidation of long-chain primary alcohols and for oxidation of S-hydroxymethyl-glutathione, a spontaneous adduct between formaldehyde and glutathione. This enzyme is an important component of cellular metabolism for the elimination of formaldehyde, a potent irritant and sensitizing agent that causes lacrymation, rhinitis, pharyngitis, and contact dermatitis. The human genome contains several non-transcribed pseudogenes related to this gene. [provided by RefSeq].
Gene References into function
- POZ domain of FBI1 represses transcription of ADH5.
- The structural determination of apo, binary alcohol, and inhibitory ternary FDH complexes provides new insight into the enzyme's metal-assisted catalysis and substrate-binding properties.
- Formation of a FDH-S-(hydroxymethyl)glutathione-NADH ternary complex causes movement of glutathione-dependent formaldehyde dehydrogenase catalytic domain toward the coenzyme-binding domain, and a change in active-site zinc coordination.
- No evidence that alcohol dehydrogenase 3genotype modifies risk related to alcohol and lung cancer.
- data suggest that genetic variation in S-nitrosoglutathione reductase (GSNOR) might play a role in asthma susceptibility
- A statistically significant increase of class III alcohol dehydrogenase isoenzymes was found in the sera of pancreatic cancer patients.
- Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
