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G4155

Sigma-Aldrich

β-Galactosidase from Escherichia coli

aqueous glycerol suspension, ≥500 units/mg protein (biuret)

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

form

aqueous glycerol suspension

Quality Level

specific activity

≥500 units/mg protein (biuret)

mol wt

465 kDa

storage temp.

−20°C

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1 of 4

This Item
G3153G5635G6008
form

aqueous glycerol suspension

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

mol wt

465 kDa

mol wt

465 kDa

mol wt

465 kDa

mol wt

465 kDa

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

300

Quality Level

200

Application

β-Galactosidase is used in the enzymatic assays in the synthesis of imidazolo-pyrrolidinoses.

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

Suspension in 50% glycerol, 5 mM Tris buffer salts, 5 mM magnesium chloride, 0.5 mM DTT, 0.5 mM mercaptoethanol. pH 7.4

Other Notes

Loss of enzymatic activity can occur if this enzyme is frozen. This enzyme is provided in a 50% glycerol solution and will not freeze if stored at -20° Celsius. It is not recommended that this enzyme preparation be stored in an ultracold freezer (-60 to -100° Celsius).

Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Théophile Tschamber et al.
Bioorganic & medicinal chemistry, 11(17), 3559-3568 (2003-08-07)
The syntheses of four glyco-imidazoles, which are pentose-derivatives belonging to the D-series, as well as the syntheses of their L-enantiomers, are reported. Starting from the known linear xylo, lyxo, arabino, and ribo imidazolo-pentoses in both the L- and the D-series
Olga Ermakova et al.
Brain sciences, 11(6) (2021-07-03)
Acquisition of detailed anatomical and molecular knowledge from intact biological samples while preserving their native three-dimensional structure is still a challenging issue for imaging studies aiming to unravel a system's functions. Three-dimensional micro-CT X-ray imaging with a high spatial resolution
Christophe Laumonnerie et al.
Development (Cambridge, England), 141(3), 594-603 (2014-01-23)
The establishment of anatomically stereotyped axonal projections is fundamental to neuronal function. While most neurons project their axons within the central nervous system (CNS), only axons of centrally born motoneurons and peripherally born sensory neurons link the CNS and peripheral
J W Callahan
Biochimica et biophysica acta, 1455(2-3), 85-103 (1999-11-26)
GM1 gangliosidosis and Morquio B disease are distinct disorders both clinically and biochemically yet they arise from the same beta-galactosidase enzyme deficiency. On the other hand, galactosialidosis and sialidosis share common clinical and biochemical features, yet they arise from two
A Hinek et al.
The Journal of clinical investigation, 91(3), 1198-1205 (1993-03-01)
We and others have previously shown that a 67-kD cell surface elastin/laminin-binding protein (EBP) is responsible for cell adhesion to elastin and laminin and for mediating the process of elastin fiber assembly, but the nature of this protein was unknown.

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