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
Service technique
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Escherichia coli
Quality Level
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
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.
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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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Contenu apparenté
QC Methods
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
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
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