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Merck

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:
Numéro CE :
Specific activity:
≥250 units/mg protein
Biological source:
Escherichia coli
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biological source

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


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