G5025
β-Galactosidase-biotin labeled from Escherichia coli
lyophilized powder, 350-1200 units/mg protein
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About This Item
biological source
Escherichia coli
form
lyophilized powder
specific activity
350-1200 units/mg protein
composition
Protein, ~75% E1%/280
extent of labeling
2-5 mol d-biotin per mol protein
Storage temp.
−20°C
Application
β-Galactosidase was used as a control antigen in the selection of human antibody fragments by phage display.[1]
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.[2]
Packaging
Package size based on protein content
Unit Definition
One unit will hydrolyze 1.0 μmole of o-nitrophenyl β-D-galactoside per min at pH 7.3 at 37 °C.
Physical form
Lyophilized powder containing Tris-acetate, DTT, MgCl2, and isopropyl β-D-thiogalactopyranoside
Preparation Note
Biotinylated using biotin–maleimide (B 1267) which incorporates an extended spacer.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Carol M Y Lee et al.
Nature protocols, 2(11), 3001-3008 (2007-11-17)
Here, we describe a protocol for the selection of human antibody fragments using repertoires displayed on filamentous bacteriophage. Antigen-specific clones are enriched by binding to immobilized antigen, followed by elution and repropagation of phage. After multiple rounds of binding selection
E A Bayer et al.
Analytical biochemistry, 149(2), 529-536 (1985-09-01)
A biotin-containing, thiol-specific reagent, 3-(N-maleimido-propionyl) biocytin (MPB), was synthesized and used to biotinylate various proteins via native or artificially induced sulfhydryl groups. In combination with appropriate avidin- or streptavidin-conjugated markers (i.e., fluorescent, enzyme-conjugated, electron-dense, etc.), MPB essentially constitutes a universal
D H Juers et al.
Protein science : a publication of the Protein Society, 8(1), 122-136 (1999-04-21)
Beta-galactosidase (lacZ) from Escherichia coli is a 464 kDa homotetramer. Each subunit consists of five domains, the third being an alpha/beta barrel that contains most of the active site residues. A comparison is made between each of the domains and
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