Rabbit Polyclonal beta glucuronidase (GUSB) antibody. Suitable for WB and reacts with Escherichia coli samples. Cited in 8 publications.
pH: 7.4
Preservative: 0.097% Sodium azide
Constituents: 0.0268% PBS
| WB | |
|---|---|
| Escherichia coli | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Escherichia coli | Dilution info - | Notes Staining of the beta Glucuronidase band in immunoblotting is specifically inhibited by the immunizing peptide. |
Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG) and with 4-methylumbelliferyl-glucuronide (PubMed:21051639, PubMed:23690068, PubMed:26364932, PubMed:3105604, PubMed:33664385). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme is able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract (PubMed:26364932).
gurA, gusA, b1617, JW1609, uidA, Beta-glucuronidase, GUS, Beta-D-glucuronoside glucuronosohydrolase, EcGUS, UID
Rabbit Polyclonal beta glucuronidase (GUSB) antibody. Suitable for WB and reacts with Escherichia coli samples. Cited in 8 publications.
pH: 7.4
Preservative: 0.097% Sodium azide
Constituents: 0.0268% PBS
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Beta Glucuronidase (GUS) sometimes referred to as E. coli Beta-Glucuronidase or GUS Beta is an enzyme involved in hydrolyzing the beta-D-glucuronic acid residues from the non-reducing end of glycosaminoglycans. This enzymatic function makes it vital for the breakdown and recycling of complex carbohydrates in cells. GUS has a molecular mass of approximately 290 kDa and is expressed in various tissues with high levels observed in the liver and kidneys which are integral components of excretory processes.
Beta Glucuronidase plays an important role in the lysosomal degradation of glycosaminoglycans. This process helps remove waste substances from the body effectively and deficiency in this enzyme may lead to the accumulation of undegraded molecules. Not part of a large complex GUS functions independently as a single protein catalytic unit. Researchers often employ the GUS assay to monitor its activity in analytical and clinical contexts indicating its importance in cellular metabolism research.
Beta Glucuronidase is integral to the glycosaminoglycan degradation pathway which is essential for catabolizing heparan sulfate and dermatan sulfate. This pathway is significant for cellular turnover and tissue remodeling. Related proteins within this metabolic framework include other lysosomal hydrolases such as acid alpha-glucosidase which work concertedly to maintain cellular homeostasis by degrading complex carbohydrates.
Deficient activity of Beta Glucuronidase links to mucopolysaccharidosis (MPS) specifically MPS VII also known as Sly syndrome. This genetic condition results in various systemic complications including skeletal and developmental abnormalities. The enzyme's malfunction may also relate to liver diseases as improper breakdown of glucuronides can impact liver function. Studies investigate the connection of Beta Glucuronidase with other lysosomal storage disorder proteins to better understand their collective impact on disease progression.
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