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Aldehyde oxidase produces hydrogen peroxide and, under certain conditions, can catalyze the formation of superoxide. Additionally we are shipping AOX1 Antibodies (59) and AOX1 Kits (18) and many more products for this protein.
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findings suggest that AOX1 acts as a contributor to the process of myogenesis by influencing the level of H2O2
AOX3 forms a homodimer and each monomer comprises three major domains involved in binding to the cofactors.
The recombinant aldehyde oxidase 3 was expressed and purified in a 30% active form, whereas the native aldehyde oxidase 3 is 100% active.
These data indicate that AOX1 is essential for adipogenesis and may link energy and drug metabolism.
In addition to their aldehyde oxidation activity, AAO1 and AAO3 were found to exhibit NADH oxidase activity, which likewise is associated with the production of superoxide anions.
Data show that alternative oxidase (AOX) fully restores ATP levels and prevents dopaminergic neurodegeneration.
ten novel single nucleotide polymorphisms resulting in amino acid exchanges in proximity to the FAD (show BRCA2 Proteins) site of hAOX1 (show HAO1 Proteins), were characterized.
Data suggest that metabolism (and possibly pharmacokinetics) of hypnotic nitrazepam involves liver enzymes AOX1 (aldehyde oxidase 1), NAT2 (N-acetyltransferase 2 (show NAT2 Proteins)), AADAC (arylacetamide deacetylase (show AADAC Proteins)), and CYP3A4 (cytochrome P450 3A4 (show CYP3A4 Proteins)).
Data suggest that substrate specificity of AOX1 includes GDC (show SLC25A16 Proteins)-0834, an inhibitor of Bruton's tyrosine kinase with potential non-steroidal anti-inflammatory agent activity; in liver cytosol, hydrolysis of GDC (show SLC25A16 Proteins)-0834 is primarily due to AOX1.
Methotrexate is poorly metabolized by human AOX1, in contrast to rabbit.
These results supported the possibility that XO/XD (show XDH Proteins) and AO can contribute to nitric oxide generation.
Several donors have a normal AOX1 protein level.
High AOX1 methylation was associated with biochemical recurrence in prostate cancer.
The physiological role of AOX1 remains unclear, but it is known that thiopurines belong to its substrates; AOX1 contributes to azathioprine catabolism.
hydralazine, at a concentration of 25 to 50 muM, can be used in human hepatocyte incubations to estimate the contribution of aldehyde oxidase to the hepatic clearance of drugs and other compounds.
Human population is characterized by the presence of functionally inactive hAOX1 (show HAO1 Proteins) allelic variants as well as variants encoding enzymes with different catalytic activities.
Amino acid substitution experiments reveal structural aspects of substrate specificity of AOX1.
Characterization of heat-induced AOX1 regulation in the green alga C. reinhardtii provides a framework for a more complete understanding of the function of this conserved protein.
in nitrate-grown cells, AOX (show ACOX1 Proteins) may play a dual role: (1) lowering the ubiquinone pool reduction level and (2) permitting the export of mitochondrial reducing power under the form of malate for nitrate and nitrite reduction
In the present work, we have isolated by RNA interference and characterized at the functional and the proteomic levels a Chlamydomonas reinhardtii strain devoid of the mitochondrial alternative oxidase 1 (AOX1).
Aldehyde oxidase produces hydrogen peroxide and, under certain conditions, can catalyze the formation of superoxide. Aldehyde oxidase is a candidate gene for amyotrophic lateral sclerosis.
aldehyde oxidase 1
, aldehyde oxidase structural homolog 2
, aldehyde oxidase
, aldehyde oxidase (female form)
, aldehyde oxidase 2
, retinal oxidase