Reactive species
Human;Rat;Mouse
Protein name
Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase (XD) (EC 1.17.1.4); Xanthine oxidase (XO) (EC 1.17.3.2) (Xanthine oxidoreductase) (XOR)]
Immunogen
Synthesized peptide derived from part region of human protein
Specificity
XDH Monoclonal Antibody detects endogenous levels of protein.
Constitute
Liquid in PBS containing 50% glycerol, and 0.02% sodium azide.
Source
Monoclonal, Mouse,IgG
Dilution rate
WB 1:500-2000
Purification process
The antibody was affinity-purified from mouse antiserum by affinity-chromatography using epitope-specific immunogen.
Background
Xanthine dehydrogenase belongs to the group of molybdenum-containing hydroxylases involved in the oxidative metabolism of purines. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Xanthine dehydrogenase can be converted to xanthine oxidase by reversible sulfhydryl oxidation or by irreversible proteolytic modification. Defects in xanthine dehydrogenase cause xanthinuria, may contribute to adult respiratory stress syndrome, and may potentiate influenza infection through an oxygen metabolite-dependent mechanism. [provided by RefSeq, Jan 2014],
Function
catalytic activity:Hypoxanthine + NAD(+) + H(2)O = xanthine + NADH.,catalytic activity:Xanthine + H(2)O + O(2) = urate + H(2)O(2).,catalytic activity:Xanthine + NAD(+) + H(2)O = urate + NADH.,cofactor:Binds 2 2Fe-2S clusters.,cofactor:FAD.,cofactor:Molybdopterin.,disease:Defects in XDH are the cause of xanthinuria type 1 (XU1) [MIM:278300]. Xanthinuria is characterized by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones. Uric acid is strikingly diminished in serum and urine. XU1 is due to isolated xanthine dehydrogenase. XU1 patients can metabolize allopurinol.,disease:May contribute to adult respiratory stress syndrome (ARDS) and may potentiate influenza infection through an oxygen metabolite-dependent mechanism.,function:This enzyme can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reve
