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ADH5 encodes a member of the alcohol dehydrogenase family. Additionally we are shipping Alcohol Dehydrogenase 5 (Class III), chi Polypeptide Proteins (36) and Alcohol Dehydrogenase 5 (Class III), chi Polypeptide Kits (4) and many more products for this protein.
Showing 10 out of 98 products:
Human Polyclonal ADH5 Primary Antibody for ELISA, WB - ABIN188741
Adinolfi, Adinolfi, Hopkinson: Immunological and biochemical characterization of the human alcohol dehydrogenase chi-ADH isozyme. in Annals of human genetics 1984
It was concluded that in HepG2 cells, ADH5 is a source of formate for de novo purine biosynthesis, especially during folate deficiency when folate-dependent formate production is limited.
GSNOR expression has different effect on neuronal viability in dependence on the stimulus applied, and plays opposite roles in SH-SY5Y models of Parkinson's disease and amyotrophic lateral sclerosis
ADH5 counteracts neuronal differentiation of neural stem cells and this effect can be reversed by pharmacological inhibition of ADH5.
common ADH (show AVP Antibodies) variants conferred risk for both schizophrenia in African-Americans and autism in European-Americans.
A decrease in ADH (show AVP Antibodies) IB, rather than GSNOR, correlates with human lung cancer.
study compared individuals occupationally exposed to formaldehyde and controls to effects of XRCC3 (show XRCC3 Antibodies) Thr241Met, ADH5 Val309Ile and Asp353Glu polymorphisms; ADH5 polymorphisms did not show significant association with genotoxicity biomarkers
Data suggest that GSNOR deficiency, through dysregulated S-nitrosylation, may promote hepatocellular carcinoma, possibly by inactivating a DNA repair system.
Significant associations were found however, for reactions to alcohol with a SNP in ADH5 (rs6827292, p = .001) and a SNP just upstream of ADH5 (rs6819724, p = .0007) that is in strong LD with rs6827292.
POZ domain of FBI1 (show ZBTB7A Antibodies) represses transcription of ADH5.
The structural determination of apo (show C9orf3 Antibodies), binary alcohol, and inhibitory ternary FDH complexes provides new insight into the enzyme's metal-assisted catalysis and substrate-binding properties.
Increased GSNOR expression during aging decreases S-nitrosation of CaMKIIalpha (show CAMK2 Antibodies) and reduces CaMKIIalpha (show CAMK2 Antibodies) synaptosomal accumulation.
These data indicate a role for GSNOR in the host response to malaria infection and suggest that strategies to disrupt its activity will improve clinical outcomes.
GSNOR may act as a "brake" on skeletal muscle contractile performance under physiological conditions by modulating nitrosylation/denitrosylation balance.
Loss of GSNOR confers enhanced post-MI cardiac regenerative activity, characterized by enhanced turnover of cardiomyocytes and cardiac stem cells.
Results show that ADH5 removes endogenous formaldehyde to prevent DNA adducts, and protects with FANCD2 (show FANCD2 Antibodies), hematopoietic stem cells, hepatocytes, and nephrons from endogenous DNA damage.
S-nitrosoglutathione reductase-dependent modification of PPARgamma (show PPARG Antibodies) alters the balance between adipocyte and osteoblast differentiation and provides checkpoint regulation of the lineage bifurcation of these 2 lineages.
These findings provide novel insights into the involvement of GSNOR and S-nitrosylation in neuromuscular atrophy and neuropathic pain that are associated with pathological states.
Overexpression of ADH5 reduces both development and adult neuronal differentiation of neurons. This effect depends on the catalytic activity of ADH5 and involves ADH5-mediated denitrosation of histone deacetylase 2 (HDAC2 (show HDAC2 Antibodies)).
GSNOR appears to play a crucial role in controlling pulmonary and systemic infection by K. pneumoniae.
A critical role for GSNOR in maintaining genomic integrity.
polar auxin transport was compromised in gsnor1-3, which was correlated with universally reduced levels of PIN (show DYNLL1 Antibodies) or GFP-PIN (show DYNLL1 Antibodies) proteins in the roots of the mutant.
Collectively, our findings imply that AtGSNOR1 controls multiple genetic networks integral to plant growth and development.
Taken together, these results suggest that GSNOR1/HOT5/PAR2 plays an important role in regulating cell death in plant cells through modulating intracellular NO level.
S-nitrosoglutathione reductase is an important and widely utilized component of pathogen resistance protein signaling networks conserved in animals and plants.
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.
, formaldehyde dehydrogenase
, glutathione-dependent formaldehyde dehydrogenase
, octanol dehydrogenase
, alcohol dehydrogenase class-3
, Alcohol dehydrogenase class-3
, hypothetical protein
, S-(hydroxymethyl)glutathione dehydrogenase
, alcohol dehydrogenase (class III), chi polypeptide
, alcohol dehydrogenase class chi chain
, alcohol dehydrogenase class-III
, S-nitrosoglutathione reductase
, alcohol dehydrogenase 2
, alcohol dehydrogenase B2
, class III alcohol dehydrogenase, chi subunit
, alcohol dehydrogenase 1C (class I), gamma polypeptide
, class III alcohol dehydrogenase
, glutothione-dependent formaldehyde dehydrogenase