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MilliporeSigma

10105031001

Roche

β-Galactosidase

from E. coli overproducer

Sinónimos:

β-galactosidase

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About This Item

Comisión internacional de enzimas:
UNSPSC Code:
12352204

biological source

Escherichia coli

Quality Level

form

suspension

specific activity

~300 units/mg protein (At 37 °C with 2-nitrophenyl-β-D-galactoside as the substrate, approximately 30 U/mg at 25 °C with lactose as the substrate; standardized with BSA.)

mol wt

540 kDa

packaging

pkg of 1,500 U

manufacturer/tradename

Roche

concentration

5.00 mg/mL

technique(s)

activity assay: suitable

optimum pH

7

suitability

suitable for UV spectrophotometry and general use

application(s)

life science and biopharma

shipped in

wet ice

storage temp.

2-8°C

Categorías relacionadas

General description

β-Galactosidase or β-D-Galactoside galactohydrolase is basically a tetramer made up of identical four polypeptide chains, each constituting 1023 amino acids. It is very specific for D-galactose and requires K+ or Na+ and Mg2+ to be fully active. β-Galactosidase enzyme with an oxygen glycosidic bond catalyzes reactions with β-d-galactopyranosides.

Specificity

Cleaves terminal galactose residues that are β1,4-linked to a monosaccharide, oligosaccharide, or glycopeptide.

Application

β-galactosidase has been used in enzyme-linked immunosorbent assay (ELISA). Use β-Galactosidase to produce a calibration curve in enzymatic assays.

Quality

Contaminants: <0.01% GIDH, GPT, LDH, MDH, and oxaloacetate decarboxylase, each

Physical form

Suspension, in 3.2 M ammonium sulfate solution, pH approximately 6, crystalline

Preparation Note

The ammonium sulfate preparation is stable at 2 to 8 °C until the expiration date printed on the label. Use directly for most applications, e.g., quantitation of lactose.

In the absence of ammonium sulfate, solutions of β-galactosidase should be stabilized with Mg2+ (89 mM) and a thiol reagent (1mM β-mercaptoethanol, 1 mM dithiothreitol) [Beutler, 1984]. The thiol slows the formation of enzyme dimers resulting from intramolecular disulfide bridges.

Activator: K (50 mM) is required for activation (lactose hydrolysis).
Na (50 mM) is also an activator, particularly for hydrolysis of 2-nitrophenyl-β-D-galactopyranoside.

Other Notes

For life science research only. Not for use in diagnostic procedures.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

No data available

flash_point_c

No data available


Certificados de análisis (COA)

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Intradermal Electroporation of Naked Replicon RNA Elicits Strong Immune Responses
Johansson D X, et al.
PLoS ONE, 7(1), e29732-e29732 (2012)
Douglas H Juers et al.
Protein science : a publication of the Protein Society, 21(12), 1792-1807 (2012-09-27)
This review provides an overview of the structure, function, and catalytic mechanism of lacZ β-galactosidase. The protein played a central role in Jacob and Monod's development of the operon model for the regulation of gene expression. Determination of the crystal

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