G1875
β-Galactosidase from bovine liver
Grade III, lyophilized powder, ≥0.15 units/mg protein
Synonyme(s) :
β-D-Galactoside galactohydrolase
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About This Item
Produits recommandés
Source biologique
bovine liver
Type
Grade III
Forme
lyophilized powder
Activité spécifique
≥0.15 units/mg protein
Composition
Protein, ≥40%
Conditions d'expédition
wet ice
Température de stockage
−20°C
Catégories apparentées
Application
β-galactosidase was used in the production of a stabilized, single reagent for alcohol analysis.
Actions biochimiques/physiologiques
β-galactosidase cleaves lactose into its monosaccharide components, glucose and galactose. It also catalyses the transglycosylation of glucose into allolactose, the inducer of β-galactosidase, in a feedback loop.
Définition de l'unité
One unit will hydrolyze 1.0 μmole of o-nitrophenyl β-D-galactoside to o-nitrophenol and D-galactose per min at pH 7.3 at 37 °C.
Inhibiteur
Réf. du produit
Description
Tarif
Substrat
Réf. du produit
Description
Tarif
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (COA)
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Les clients ont également consulté
Stabilization of Analytical Enzymes Using a Novel Polymer-Carbohydrate System and the Production of a Stabilized, Single Reagent for Alcohol Analysis
Analyst, 117, 1293-1297 (1992)
ChemMedChem, 12(7), 483-486 (2017-03-23)
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Protein science : a publication of the Protein Society, 8(1), 122-136 (1999-04-21)
Beta-galactosidase (lacZ) from Escherichia coli is a 464 kDa homotetramer. Each subunit consists of five domains, the third being an alpha/beta barrel that contains most of the active site residues. A comparison is made between each of the domains and
Reciprocal regulation of pH 6 antigen gene loci by PhoP and RovA in Yersinia pestis biovar Microtus.
Future microbiology, 8(2), 271-280 (2013-02-05)
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Cell cycle (Georgetown, Tex.), 12(4), 555-578 (2013-02-02)
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