Urate Oxidase, Recombinant, Human (UOX)

Urate oxidase catalyzes the enzymatic oxidation of uric acid into allantoin, an inactive and soluble metabolite. Recombinant Human Urate Oxidase produced in E.Coli is a tetrameric, non-glycosylated polypeptide chain containing 301 amino acids, having a molecular formula of C1523H2383N417O462S7 and a molecular mass of 34,247 Dalton.\n\nBiological Activity: \nThe specific activity was found to be 18U/mg. One Unit oxidizes one micromole of uric acid per minute at 30 degrees C, at pH 8.9.\n\nAmino Acid Sequence: \nmsavkaaryg kdnvrvykvh kdektgvqtv yemtvcvlle geietsytka dnsvivatds ikntiyitak qnpvtppelf gsilgthfie kynhihaahv nivchrwtrm didgkphphs firdseekrn vqvdvvegkg idiksslsgl tvlkstnsqf wgflrdeytt lketwdrils tdvdatwqwk nfsglqevrs hvpkfdatwa tarevtlktf aednsasvqa tmykmaeqil arqqlietve yslpnkhyfe idlswhkglq ntgknaevfa pqsdpnglik ctvgrsslks kl\n\nEndotoxin: \nLess than 10 ng/1.5mg of Urate Oxidase.\n\nSolubility: \nIt is recommended to reconstitute the lyophilized Recombinant UOX in sterile 18MOmega-cm H2O not less than 100microg/ml, which can then be further diluted to other aqueous solutions.\n\nStability: \nLyophilized rUOX although stable at room temperature for 3 weeks, should be stored desiccated below -180C. Upon reconstitution Recombinant UOX should be stored at 40C between 2-7 days and for future use below -180C. Please prevent freeze-thaw cycles.

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SPECIFICATIONS

Catalog Number

U2004-75

Size

100ug

Form

Supplied as a white lyophilized powder. Each 1.5mg urate oxidase contains 5mg sucrose, 25mg glycine, 0.1mg Tween-80, 13.6mg Na2HPO4

Purity

(same/more than) 95% as determined by RP-HPLC, anion-exchange FPLC and/or reducing and non-reducing SDS-PAGE Silver Stained gel.

References

1. (2006) FEBS Lett Apr 3;580(8):2087-91. 2. (2006) Acta Crystallograph Sect F Struct Biol Cryst Commun Mar 1;62(Pt 3):306-9. 3. (2006) Biochim Biophys Acta Mar;1764(3):391-7. 4. (2005) Curr Drug Discov Technol Mar;2(1):29-36. 5. (2006) Acta Haematol 115(1-2):35-8. 6. (2005)J Electron Microsc (Tokyo) Aug;54(4):385-92.