G1875
β-Galactosidase from bovine liver
Grade III, lyophilized powder, ≥0.15 units/mg protein
동의어(들):
β-D-Galactoside galactohydrolase
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크기 선택
보기 변경
제품정보 (DICE 배송 시 비용 별도)
CAS 번호:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-864-1
MDL number:
Specific activity:
≥0.15 units/mg protein
Biological source:
bovine liver
biological source
bovine liver
Quality Level
type
Grade III
form
lyophilized powder
specific activity
≥0.15 units/mg protein
composition
Protein, ≥40%
shipped in
wet ice
storage temp.
−20°C
Application
β-galactosidase was used in the production of a stabilized, single reagent for alcohol analysis.
Biochem/physiol Actions
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.
Other Notes
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.
저장 등급
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
관련 콘텐츠
QC Methods
Stabilization of Analytical Enzymes Using a Novel Polymer-Carbohydrate System and the Production of a Stabilized, Single Reagent for Alcohol Analysis
Timothy D. Gibson, John Higgins, John R. Woodward
Analyst, 117, 1293-1297 (1992)
Alen Sevšek et al.
ChemMedChem, 12(7), 483-486 (2017-03-23)
A series of lipidated guanidino and urea derivatives of 1,5-dideoxy-1,5-imino-d-xylitol were prepared from d-xylose using a concise synthetic protocol. Inhibition assays with a panel of glycosidases revealed that the guanidino analogues display potent inhibition against human recombinant β-glucocerebrosidase with IC50
D H Juers et al.
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