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G4259

Sigma-Aldrich

β-Glucuronidase from Helix aspersa (garden snail)

Type HA-4

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About This Item

Classificazione EC (Enzyme Commission):
Numero CE:
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54

Tipo

Type HA-4

Forma fisica

partially purified powder

Attività specifica

≥300,000 units/g solid solid

secondary activity

≤7,500 units/g solid sulfatase

Solubilità

H2O: soluble 1.90-2.10 mg/mL, clear to slightly hazy

applicazioni

clinical testing

Temperatura di conservazione

−20°C

Applicazioni

β-glucuronidase was used in enzymic hydrolysis of tissue homogenates for liquid chromatography-electrospray ion trap mass spectrometry (LC/MSn) analysis, to study the structures of degradation products of baicalin.

Azioni biochim/fisiol

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.

Definizione di unità

One Sigma or modified Fishman unit will liberate 1.0 μg of phenolphthalein from phenolphthalein glucuronide per hr at 37°C at the pH 5.0 (30 min assay).
One unit of sulfatase will hydrolyze 1.0 μmole p-nitrocatechol sulfate per hr at pH 5.0 at 37 °C.

Altre note

Used for the hydrolysis of glucuronide conjugates in urinary metabolite analysis

Substrato

Pittogrammi

Health hazard

Avvertenze

Danger

Indicazioni di pericolo

Consigli di prudenza

Classi di pericolo

Resp. Sens. 1 - Skin Sens. 1

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


Certificati d'analisi (COA)

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Vectors with the gus reporter gene for identifying and quantitating promoter regions in <I>Saccharomyces cerevisiae</I>
Marathe &amp; J.E. McEwen
Gene, 154, 105-107 (1988)
J D McCarter et al.
Current opinion in structural biology, 4(6), 885-892 (1994-12-01)
The determination of a large number of three-dimensional structures of glycosidases, both free and in complex with ligands, has provided valuable new insights into glycosidase catalysis, especially when coupled with results from studies of specifically labelled glycosidases and kinetic analyses
S Jain et al.
Nature structural biology, 3(4), 375-381 (1996-04-01)
The X-ray structure of the homotetrameric lysosomal acid hydrolase, human beta-glucuronidase (332,000 Mr), has been determined at 2.6 A resolution. The tetramer has approximate dihedral symmetry and each promoter consists of three structural domains with topologies similar to a jelly
Catalytic mechanisms of enymatic glycosyl transfer
M.L. Sinnott
Chemical Reviews, 90, 1171-1202 (1990)
Jie Xing et al.
Journal of pharmaceutical and biomedical analysis, 39(3-4), 593-600 (2005-05-17)
The stability of baicalin in buffered aqueous solutions at different pHs and in biological fluids, including plasma, urine and tissue homogenates, were investigated in vitro. Structures of the degradation products of baicalin were elucidated by liquid chromatography-electrospray ion trap mass

Protocolli

Enzymatic assay protocol for β-Glucuronidase from Helix Pomatia and Bovine Liver aids laboratory personnel in following procedures.

Optimize β-glucuronidase hydrolysis for glucuronide metabolite analysis considering factors like time, temperature, pH, and enzyme concentration.

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