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Key Documents

G6048

Sigma-Aldrich

Galactokinase human

recombinant, expressed in E. coli

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About This Item

Enzyme Commission number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

form

solution

specific activity

≥1400 unit/μg protein

mol wt

42 kDa

shipped in

dry ice

storage temp.

−70°C

Biochem/physiol Actions

Galactokinase catalyzes the phosphorylation of αD-galactose to produce galactose-1-phosphate as part of the Leloir pathway.

Physical properties

N-terminal GST-tagged 42 kDa full length protein

Unit Definition

One unit will convert 1.0 picomole of galactose to galactose-1-phosphate per minute at pH 7.4 at 30 °C.

Physical form

Supplied as a solution in 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 20% glycerol, 3 mM DTT and 10-250 mM imidazole.

Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2

Storage Class Code

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Aurélie Egert et al.
Plant & cell physiology, 53(5), 921-929 (2012-03-23)
Galactokinase (GALK, EC 2.7.1.6) is a cytosolic enzyme with a wide occurrence across the taxonomic kingdoms. It catalyzes the phosphorylation of α-d-galactose (Gal) to α-d-Gal-1-P. The cytotoxicity of free (unphosphorylated) Gal is well documented in plants and causes marked defects.
Erin M Green et al.
Molecular biology of the cell, 23(7), 1367-1375 (2012-02-11)
The genome is nonrandomly organized within the nucleus, but it remains unclear how gene position affects gene expression. Silenced genes have frequently been found associated with the nuclear periphery, and the environment at the periphery is believed to be refractory
Nils Janzen et al.
Archives of medical research, 42(7), 608-612 (2011-12-14)
Galactokinase (GALK) deficiency is an autosomal recessive disorder causing cataract formation that can be prevented or mitigated by early diagnosis and galactose-restricted diet. The aim of this retrospective study was to explore whether GALK-deficiency meets the criteria for neonatal mass
Tali Lavy et al.
Genes & development, 26(3), 294-303 (2012-02-04)
A wealth of genetic information and some biochemical analysis have made the GAL regulon of the yeast Saccharomyces cerevisiae a classic model system for studying transcriptional activation in eukaryotes. Galactose induces this transcriptional switch, which is regulated by three proteins:
Lei Li et al.
Carbohydrate research, 355, 35-39 (2012-05-29)
Galactokinase (GalK), particularly GalK from Escherichia coli, has been widely employed for the synthesis of sugar-1-phosphates. In this study, a GalK from Bifidobacterium infantis ATCC 15697 (BiGalK) was cloned and over-expressed with a yield of over 80 mg/L cell cultures.

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