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Merck
CN

G5635

Sigma-Aldrich

β-Galactosidase from Escherichia coli

Grade VIII, lyophilized powder, ≥500 units/mg protein

Synonym(s):

β-D-Galactoside galactohydrolase, Lactase

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About This Item

CAS Number:
9031-11-2
EC Number:
3.2.1.23 (BRENDA, IUBMB)
EC Number:
232-864-1
MDL number:
MFCD00155434
UNSPSC Code:
12352204
NACRES:
NA.54

Key Documents

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type

Grade VIII

Quality Level

300

form

lyophilized powder

specific activity

≥500 units/mg protein

mol wt

465 kDa

does not contain

BSA as extender

composition

Protein, ≥60% biuret

storage temp.

−20°C

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General description

β-Galactosidase is a tetramer consisting of four equal subunits of 135,000 each. It is a sulfhydryl containing enzyme, with 19 cysteine residues per subunit.
Tetramer molecular weight 465 kDa (subunits 116.3 kDa each)

Application

β-Galactosidase is conjugated to an antibody which 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. It may be used as a positive control protein with anti-β-galactosidase antibodies.

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.

Physical form

Contains Tris buffer salts and magnesium chloride

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
0000477705
0000477705
0000477706
0000477707
0000477704

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Alan Merk et al.
IUCrJ, 7(Pt 4), 639-643 (2020-07-23)
We report the determination of the structure of Escherichia coli β-galactosidase at a resolution of ∼1.8 Å using data collected on a 200 kV CRYO ARM microscope equipped with a K3 direct electron detector. The data were collected in a single 24 h
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
Raimond B G Ravelli et al.
Nature communications, 11(1), 2563-2563 (2020-05-24)
The increasing demand for cryo-electron microscopy (cryo-EM) reveals drawbacks in current sample preparation protocols, such as sample waste and lack of reproducibility. Here, we present several technical developments that provide efficient sample preparation for cryo-EM studies. Pin printing substantially reduces
Assays for bacterial mucin-desulfating sulfatases.
A M Roberton et al.
Methods in molecular biology (Clifton, N.J.), 125, 417-426 (2000-05-23)
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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