β-Glucuronidase from Escherichia coli

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.

New Technical Article Comparing Performance of Different Enzymes
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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

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.

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.

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).

Highly purified solution in 50% glycerol