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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥5,000,000 units/g protein, pH 6.8 (biuret)
Biological source:
Escherichia coli
biological source
Escherichia coli
form
aqueous glycerol solution
specific activity
≥5,000,000 units/g protein, pH 6.8 (biuret)
mol wt
69-71 kDa
shipped in
wet ice
storage temp.
−20°C
Quality Level
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General description
β-Glucuronidase from Escherichia coli is similar to human glucuronidase enzyme and corresponds to molecular weight close to 69-71 kDa and has an pH optimum of 6.5-7.5. It belongs to family-2 glycosyl hydrolase and has active site residues glutamic acid 394, tyrosine 468 and glutamic acid 504.
Application
β-Glucuronidase from Escherichia coli has been used in the enzymatic cleavage and activation of glucuronide prodrugs in non-small cell lung cancer cells, U87 human glioblastoma cell line, in A549 (human lung adenocarcinoma) and KB (human oral squamous carcinoma).
β-Glucuronidase from E. coli is used for the enzymatic hydrolysis of b-glucuronides in urine and other fluids. It has a high rate of hydrolytic activity and may be useful for determining the presence of androsterone, 17-hydroxycorticosteroids, and estriol in urine.
The optimal conditions for the enzymatic hydrolysis of α-hydroxytriazolam, one of the major metabolites of triazolam in human urine, were determined using β-glucuronidase Type IX-A.
It is used as a reporter gene in GUS assays to monitor gene expression.
The optimal conditions for the enzymatic hydrolysis of α-hydroxytriazolam, one of the major metabolites of triazolam in human urine, were determined using β-glucuronidase Type IX-A.
It is used as a reporter gene in GUS assays to monitor gene expression.
New 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
Effective in the hydrolysis of steroid glucuronides.
Used for the hydrolysis of glucuronide conjugates in urinary metabolite analysis
Biochem/physiol Actions
β-Glucuronidase catalyzes the hydrolysis of β-glucuronic acid residues from the non-reducing termini of glycosaminoglycans (GAGs). β-Glucuronidase is a potential candidate enzyme for gene-mediated enzyme prodrug therapy for glucuronide prodrugs. Use of β-Glucuronidase-albumin complex based drug delivery could be an effective therapeutic methodology for treating solid tumors.
β-glucuronidase (β-GIc) is an exoglycosidase that catalyzes the breakdown of complex carbohydrates. In humans it converts conjugated bilirubin into the unconjugated form, making bilirubin suitable for reabsorption.
Physical form
Highly purified solution in 50% glycerol
Other Notes
One Sigma or modified Fishman unit will liberate 1.0 μg of phenolphthalein from phenolphthalein glucuronide per hr at 37 °C at the pH 6.8 (30 min assay).
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Membrane-localized activation of glucuronide prodrugs by beta-glucuronidase enzymes
Chen KC, et al.
Cancer Gene Therapy, 14(2), 187-187 (2007)
Mickaël Thomas et al.
Bioorganic & medicinal chemistry, 16(17), 8109-8116 (2008-08-12)
Two glucuronide prodrugs of the histone deacetylase inhibitor CI-994 were synthesized. These compounds were found to be soluble in aqueous media and stable under physiological conditions. The carbamoyl derivatisation of CI-994 significantly decreased its toxicity towards NCI-H661 lung cancer cells.
Synthesis and biological evaluations of a monomethylauristatin E glucuronide prodrug for selective cancer chemotherapy
Legigan T, et al.
European Journal of Medicinal Chemistry, 67, 75-80 (2013)
Expression and Purification of Escherichia coli beta-Glucuronidase
Aich S, et al.
Protein Expression and Purification, 22(1), 75-81 (2001)
Study of a cyclopamine glucuronide prodrug for the selective chemotherapy of glioblastoma
Hamon F, et al.
European Journal of Medicinal Chemistry, 45(4), 1678-1682 (2010)
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