SRE0023
β-Glucuronidase from abalone
Purified, aqueous solution, β-glucuronidase 150,000-250,000 units/mL, β-glucuronidase ≥20,000,000 units/g protein
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About This Item
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Quality Level
form
aqueous solution
β-glucuronidase activity
≥20,000,000 units/g protein
150,000-250,000 units/mL
secondary activity
≤7,500 units/mL sulfatase
storage temp.
2-8°C
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Application
Technical Article Comparing Performance of Different Enzymes
Learn more
about recent application data generated by Sigma R&D to optimize hydrolysis for different drug classes using enzymes from different sources and the use of a chromatographicaly purified enzyme to reduce the effect of esterase activity resulting in conversion of 6-MAM to Morphine.
Learn more
about recent application data generated by Sigma R&D to optimize hydrolysis for different drug classes using enzymes from different sources and the use of a chromatographicaly purified enzyme to reduce the effect of esterase activity resulting in conversion of 6-MAM to Morphine.
Biochem/physiol Actions
β-Glucuronidase (GUSB) is a lysosomal enzyme, that degrades glucuronate-containing glycosaminoglycans. β-glucuronidase, obtained from abalone has the ability to hydrolyze samples, that has high analyte concentrations. Absence of β-glucuronidase results in mucopolysaccharidosis type VII (MPSVII), which leads to lysosomal storage in the brain.
Unit Definition
One Sigma or modified Fishman unit will liberate 1.0 μg of phenolphthalein from phenolphthalein glucuronide per hr at 37 °C at pH 3.8 (30 min assay).
Physical form
Supplied as an aqueous solution containing L-proline, ammonium acetate and sodium azide
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Evaluation of abalone beta-glucuronidase substitution in current urine hydrolysis procedures
Journal of Analytical Toxicology, 38(3), 171-176 (2014)
Human beta-glucuronidase: structure, function, and application in enzyme replacement therapy
Rejuvenation Research, 16(5), 352-363 (2013)
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