Active • Source: Raw bovine milk • AA: 1-1,332 (full length) • MW: 146.79 kDa
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Xanthine Oxidase (bovine)

Item No. 38017

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • Xanthine Dehydrogenase/Oxidase
  • Xanthine Oxidoreductase
  • XO
  • XOR
Source
Active xanthine oxidase purified from raw bovine milk
Amino Acids
1-1,332
MW
146.79
Formulation (Request formulation change)
2.3 M of ammonium sulfate with 10 mM sodium phosphate, pH 7.8, 1 mM EDTA and 1 mM sodium salicylate
Shipping & Storage Information
Storage
4°C
Shipping
Room temperature in continental US; may vary elsewhere
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    1 U

    $165

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    Cayman Chemical
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    OBESITY RESEARCH SOLUTIONS
    Product Description

    Xanthine oxidase (XO) is a complex metalloflavoprotein involved in purine catabolism, oxidative stress, and xenobiotic metabolism, among other processes.1,2 It exists as a homodimer and each monomer is composed of an N-terminal domain that contains two unequal iron-sulfur clusters, an intermediate domain that contains the FAD cofactor, and a C-terminal domain that contains the molybdopterin cofactor. XO is primarily expressed in the liver and intestines, has been found in blood, serum, and milk, and localizes to the cytosol, cell membrane, and peroxisomes.1 It is produced by irreversible or reversible post-translational modification of xanthine dehydrogenase (XD) via limited proteolysis or oxidation of XD thiol groups, respectively.1,2 XO catalyzes the conversion of hypoxanthine to xanthine to uric acid and uses molecular oxygen as the electron acceptor, compared with XD that uses NAD+, and this results in the generation of hydrogen peroxide and superoxide, which can react with nitric oxide (NO) to produce peroxynitrite.1,2,3 In hypoxic conditions, XO converts nitrates and nitrite to NO.4 Increased blood levels of XO’s enzymatic product uric acid, hyperuricemia, is associated with several diseases, including gout, cardiovascular disease, ischemia-reperfusion injury, obesity, and diabetes.1,2,5,6,7 XO has commonly been used in coupled enzyme assays to measure superoxide dismutase (SOD) activity.8,9 Cayman’s Xanthine Oxidase (bovine) protein can be used for enzyme activity assays.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Battelli, M.G., Bolognesi, A., and Polito, L. Pathophysiology of circulating xanthine oxidoreductase: New emerging roles for a multi-tasking enzyme. Biochim. Biophys. Acta 1842(9), 1502-1517 (2014).

    2. Battelli, M.G., Bortolotti, M., Bolognesi, A., et al. Pro-aging effects of xanthine oxidoreductase products. Antioxidants (Basel) 9(9), 839 (2020).

    3. Lee, C., Liu, X., and Zweier, J.L. Regulation of xanthine oxidase by nitric oxide and peroxynitrite. The Journal of Biological Chemisty 275(13), 9369-9376 (2000).

    4. Millar, T.M., Stevens, C.R., Benjamin, N., et al. Xanthine oxidoreductase catalyses the reduction of nitrates and nitrite to nitric oxide under hypoxic conditions. FEBS Lett. 427, 225-228 (1998).

    5. Garcia-Gil, M., Camici, M., Allegrini, S., et al. Emerging role of purine metabolizing enzymes in brain function and tumors. Int. J. Mol. Sci. 19(11), 3598 (2018).

    6. Dawson, J., and Walters, M. Uric acid and xanthine oxidase: Future therapeutic targets in the prevention of cardiovascular disease? Br. J. Clin. Pharmac. 62(6), 633-644 (2006).

    7. Glantzounis, G.K., Tsimoyiannis, E.C., Kappas, A.M., et al. Uric acid and oxidative stress. Curr. Pharm. Des. 11(32), 4145-4151 (2005).

    8. Sun, Y., Oberley, L.W., and Li, Y. A simple method for clinical assay of superoxide dismutase. Clin. Chem. 34(3), 497-500 (1988).

    9. Okado-Matsumoto, A., and Fridovich, I. Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu, Zn-SOD in mitochondria. The Journal of Biological Chemisty 276(46), 38388-38393 (2001).