G6008
β-Galactosidase from Escherichia coli
Grade VI, lyophilized powder, ≥250 units/mg protein
Synonyme(s) :
β-D-Galactoside galactohydrolase, Lactase
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-864-1
MDL number:
Specific activity:
≥250 units/mg protein
Biological source:
Escherichia coli
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Laissez-nous vous aiderbiological source
Escherichia coli
type
Grade VI
form
lyophilized powder
specific activity
≥250 units/mg protein
mol wt
465 kDa
does not contain
BSA as extender
composition
Protein, ≥50% biuret
shipped in
wet ice
storage temp.
−20°C
Quality Level
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Catégories apparentées
General description
Poids moléculaire du tétramère : 465 kDa (chaque sous-unité ayant 116,3 kDa)
β-Galactosidase is a tetramer consisting of four equal subunits of 135,000 Da each. It is a sulfhydryl containing enzyme, with 19 cysteine residues per subunit.
Application
β-Galactosidase is conjugated to an antibody that specifically recognizes a target molecule (enzyme immunoassay or EIA). β-Galactosidase is also used as a reporter enzyme to monitor the level of gene expression of a promoter.
Biochem/physiol Actions
βLa β-galactosidase clive le lactose en ses constituants monosaccharides, le glucose et le galactose. Elle catalyse également la transglycosylation du glucose en allolactose, inducteur de la β-galactosidase, dans une boucle de rétroaction.
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.
Physical form
Partially purified; contains Tris buffer salts, magnesium chloride, DL-dithiothreitol and 2-mercaptoethanol
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.
wgk
WGK 3
Classe de stockage
11 - Combustible Solids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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David P Klebl et al.
Frontiers in molecular biosciences, 9, 945772-945772 (2022-08-23)
Advances in single particle cryo-EM data collection and processing have seen a significant rise in its use. However, the influences of the environment generated through grid preparation, by for example interactions of proteins with the air-water interface are poorly understood
K Kato et al.
Journal of immunology (Baltimore, Md. : 1950), 116(6), 1554-1560 (1976-06-01)
1. A method for the conjugation of the Fab' fragment of rabbit IgG with beta-D-galactosidase from Escherichia coli is described. The method consists of two main steps: treatment of the Fab' fragments containing sulfhydryl groups with excess N,N'-o-phenylenedimaleimide, to introduce
D C Young et al.
Analytical biochemistry, 215(1), 24-30 (1993-11-15)
Bacterial beta-galactosidase is one of several reporter enzymes used in studying the transcriptional activity of eukaryotic promoters. Although it is one of the easiest and least expensive enzymes to assay, its use has been limited because of its low sensitivity
Orit Redy-Keisar et al.
Nature protocols, 9(1), 27-36 (2013-12-07)
This protocol describes the synthesis of modular turn-ON QCy7-based probes for the detection of biologically relevant analytes, such as hydrogen peroxide, ubiquitous sulfhydryl and β-galactosidase. The probes presented herein are prepared through a simple procedure that involves the preliminary alkylation
PURIFICATION, COMPOSITION, AND MOLECULAR WEIGHT OF THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12.
G R CRAVEN et al.
The Journal of biological chemistry, 240, 2468-2477 (1965-06-01)
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