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G3153

Sigma-Aldrich

β-Galactosidase from Escherichia coli

lyophilized powder, ≥500 units/mg protein

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Synonym(s):
β-D-Galactoside galactohydrolase, Lactase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

form

lyophilized powder

specific activity

≥500 units/mg protein

mol wt

465 kDa

storage temp.

−20°C

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This Item
G6008G4155345788
form

lyophilized powder

form

lyophilized powder

form

aqueous glycerol suspension

form

lyophilized solid

specific activity

≥500 units/mg protein

specific activity

≥250 units/mg protein

specific activity

≥500 units/mg protein (biuret)

specific activity

≥600 units/mg protein

mol wt

465 kDa

mol wt

465 kDa

mol wt

465 kDa

mol wt

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

General description

β-galactosidase is a 465 kDa tetrameric protein. It is coded by the LacZ gene.

Application

β-Galactosidase from Escherichia coli has been used to produce biocatalytic Ca-alginate beads on a B-390 encapsulator (BUCHI). It has been used to prepare the source droplet solution and also as the cargo for Pep-1 (KETWWETWWTEWSQPKKKRKV-cysteamide).
β-Galactosidase may be used for derivatization, such as an enzyme label for IgG, without prior dialysis or gel filtration.

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.
β-galactosidase is considered as a reporter enzyme in applications involving gene expression regulation, analysis of protein function/structure and target gene expression.

Packaging

Package size based on protein content

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-galactopyranoside to o-nitrophenol and D-galactose per min at pH 7.3 at 37 °C.

Physical form

Stabilized with phosphate buffer and sucrose

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

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Customers Also Viewed

Samuel Berhanu et al.
Journal of basic microbiology, 62(6), 669-688 (2022-03-16)
pUC18 and pUC19 are well-known high copy-number plasmid vectors routinely used for DNA cloning purposes. We show here that, in Escherichia coli transformed by native pUC18, the α-complementation of β-galactosidase (i.e., mediated by the peptide LacZα18) is intrinsically weak and
M J O'Sullivan et al.
Annals of clinical biochemistry, 16(5), 221-240 (1979-09-01)
In the last few years, the use of enzyme labels in immunoassays has been investigated. The aim of this review is to evaluate critically the role of such labels in clinical biochemistry. Special attention has been given to the problems
Structure of beta-galactosidase at 3.2-AA resolution obtained by cryo-electron microscopy
Bartesaghi A, et al.
Proceedings of the National Academy of Sciences of the USA, 111(32), 11709-11709 (2014)
Peptide-Mediated Membrane Transport of Macromolecular Cargo Driven by Membrane Asymmetry
Li X, et al.
Analytical Chemistry, 89(22), 12369-12374 (2017)
Application of galactose-sensitive E. coli strains as selective hosts for LacZ-plasmids.
Gossen JA, et al.
Nucleic Acids Research, 20(12), 3254-3254 (1992)

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