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Key Documents

Safety Information

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:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

type

Grade VIII

Quality Level

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.

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 properties

Tetramer molecular weight 465 kDa (subunits 116.3 kDa each)

Unit Definition

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.

Physical form

Contains Tris buffer salts and magnesium chloride

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 Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

G5635-5KU-PW:
G5635-RSAMPLE:
G5635-15KU:
G5635-VAR:
G5635-BULK:
G5635-15KU-PW:
G5635-1KU-PW:
G5635-3KU-PW:
G5635-1KU:
G5635-5KU:
G5635-3KU:


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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)
Assays for bacterial mucin-desulfating sulfatases.
A M Roberton et al.
Methods in molecular biology (Clifton, N.J.), 125, 417-426 (2000-05-23)
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
Toshiya Suzuki et al.
Plant physiology, 173(1), 183-205 (2016-11-12)
Pollen exine is essential for protection from the environment of the male gametes of seed-producing plants, but its assembly and composition remain poorly understood. We previously characterized Arabidopsis (Arabidopsis thaliana) mutants with abnormal pollen exine structure and morphology that we

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