G8162
β-Glucuronidase from Escherichia coli
aqueous glycerol solution, ≥5,000,000 units/g protein, pH 6.8 (biuret)
Synonym(s):
β-D-Glucuronide glucuronosohydrolase
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About This Item
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biological source
Escherichia coli
Quality Level
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
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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.
Unit Definition
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).
Physical form
Highly purified solution in 50% glycerol
comparable product
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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beta-Glucuronidase-responsive prodrugs for selective cancer chemotherapy: an update
European Journal of Medicinal Chemistry, 74, 302-313 (2014)
Study of a cyclopamine glucuronide prodrug for the selective chemotherapy of glioblastoma
European Journal of Medicinal Chemistry, 45(4), 1678-1682 (2010)
Membrane-localized activation of glucuronide prodrugs by beta-glucuronidase enzymes
Cancer Gene Therapy, 14(2), 187-187 (2007)
Expression and Purification of Escherichia coli beta-Glucuronidase
Protein Expression and Purification, 22(1), 75-81 (2001)
Synthesis and biological evaluations of a monomethylauristatin E glucuronide prodrug for selective cancer chemotherapy
European Journal of Medicinal Chemistry, 67, 75-80 (2013)
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