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X3128

Sigma-Aldrich

Xanthine Agarose

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NACRES:
NA.56

matrix

4% cross-linked agarose

capacity

≥1.5 mg/mL binding capacity (uricase)

storage temp.

2-8°C

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This Item
M026910110434001900957
Sigma-Aldrich

Sigma-Aldrich

X3128

Xanthine Agarose

Sigma-Aldrich

Sigma-Aldrich

M0269

Methotrexate−Agarose

Xanthine Oxidase (XOD) from cow milk

Roche

10110434001

Xanthine Oxidase (XOD)

Azide agarose

Sigma-Aldrich

900957

Azide agarose

capacity

≥1.5 mg/mL binding capacity (uricase)

capacity

-

capacity

-

capacity

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

200

Quality Level

200

Quality Level

100

Quality Level

100

Application

Xanthine-agarose is used for protein chromatography, affinity chromatography and specialty resins. Xanthine-agarose has been used to purify and determine molecular properties of urate oxidase from Chlamydomonas reinhardtii. Xanthine-agarose has also been used to determine physicochemical properties and states of sulfhydryl groups of uricase from Candida utilis.

Pictograms

Flame
GHS02

Signal Word

Warning

Hazard Statements

H226

Hazard Classifications

Flam. Liq. 3

Storage Class Code

3 - Flammable liquids

WGK

WGK 2

Flash Point(F)

102.9 °F - closed cup

Flash Point(C)

39.4 °C - closed cup

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705578-5MG-PW

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MMYOMAG-74K-13

1000309185

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Uric acid ≥99%, crystalline

Sigma-Aldrich

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S S Mösli Waldhauser et al.
Phytochemistry, 45(7), 1407-1414 (1997-08-01)
Caffeine biosynthesis comprises sequential methylations at N-7, N-3 and N-1 of the xanthine ring catalysed by S-adenosyl-L-methionine (SAM)-dependent methyltransferase activities that, to date, have not been resolved. Enzyme extracts were prepared from young, emerging coffee leaflets and following anion exchange
Débora da Silva Freitas et al.
International journal of pharmaceutics, 387(1-2), 215-222 (2009-12-09)
PEGylation is a successful strategy for improving the biochemical and biopharmaceutical properties of proteins and peptides through the covalent attachment of polyethylene glycol chains. In this work, purified recombinant uricase from Candida sp. (UC-r) was modified by PEGylation with metoxypolyethilenoglycol-p-nitrophenyl-carbonate
Isolation and characterization of uricase from bean leaves and its comparison with uredospore enzymes.
Montalbini, P., et al.
Plant Science, 147(2), 139-147 (1999)
Uricase from leaves: its purification and characterization from three different higher plants.
Montalbini, P., et al.
Planta, 202(3), 277-283 (1997)
Miguel Aguilar et al.
Current microbiology, 44(4), 257-261 (2002-03-23)
Uricase (urate: oxygen oxidoreductase; EC 1.7.3.3) from the rust Puccinia recondita was purified to electrophoretic homogeneity. Preparations with a specific activity of 8.4 U/mg were used for characterization of the enzyme, which showed a strong similarity to other plant and
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