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Key Documents

X3128

Sigma-Aldrich

Xanthine Agarose

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About This Item

UNSPSC Code:
41106500
NACRES:
NA.56

matrix

4% cross-linked agarose

capacity

≥1.5 mg/mL binding capacity (uricase)

storage temp.

2-8°C

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

signalword

Warning

hcodes

Hazard Classifications

Flam. Liq. 3

Storage Class

3 - Flammable liquids

wgk_germany

WGK 2

flash_point_f

102.9 °F - closed cup

flash_point_c

39.4 °C - closed cup


Certificados de análisis (COA)

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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
Uricase from leaves: its purification and characterization from three different higher plants.
Montalbini, P., et al.
Planta, 202(3), 277-283 (1997)
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)
Marialaura Marchetti et al.
Scientific reports, 6, 38302-38302 (2016-12-07)
Urate oxidase (Uox) catalyses the first reaction of oxidative uricolysis, a three-step enzymatic pathway that allows some animals to eliminate purine nitrogen through a water-soluble compound. Inactivation of the pathway in hominoids leads to elevated levels of sparingly soluble urate
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

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