X3128
Xanthine Agarose
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About This Item
NACRES:
NA.56
UNSPSC Code:
41106500
matrix
4% cross-linked agarose
capacity
≥1.5 mg/mL binding capacity (uricase)
storage temp.
2-8°C
Quality Level
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.
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Warning
hcodes
Hazard Classifications
Flam. Liq. 3
Storage Class
3 - Flammable liquids
wgk
WGK 2
flash_point_f
102.9 °F - closed cup
flash_point_c
39.4 °C - closed cup
Regulatory Information
危险化学品
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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
Uricase from leaves: its purification and characterization from three different higher plants.
Montalbini, P., et al.
Planta, 202(3), 277-283 (1997)
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
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
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)
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