G3153
β-Galactosidase from Escherichia coli
lyophilized powder, ≥500 units/mg protein
Synonym(s):
β-D-Galactoside galactohydrolase, Lactase
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About This Item
Recommended Products
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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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
inhibitor
Product No.
Description
Pricing
substrate
Product No.
Description
Pricing
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
Certificates of Analysis (COA)
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Structure of beta-galactosidase at 3.2-AA resolution obtained by cryo-electron microscopy
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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
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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
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