G6637
β-Galactose Dehydrogenase from Pseudomonas fluorescens
recombinant, expressed in E. coli, ammonium sulfate suspension, ≥50 units/mg protein (biuret)
Synonyme(s) :
D-Galactose:NAD+ 1-oxidoreductase
Se connecter pour consulter les tarifs organisationnels et contractuels.
Sélectionner une taille de conditionnement
A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-837-4
MDL number:
Specific activity:
≥50 units/mg protein (biuret)
Assay:
0.5—2.0 mg protein/mL (biuret)
Biological source:
Pseudomonas fluorescens
Recombinant:
expressed in E. coli
Service technique
Besoin d'aide ? Notre équipe de scientifiques expérimentés est là pour vous.
Laissez-nous vous aiderService technique
Besoin d'aide ? Notre équipe de scientifiques expérimentés est là pour vous.
Laissez-nous vous aiderbiological source
Pseudomonas fluorescens
recombinant
expressed in E. coli
assay
0.5—2.0 mg protein/mL (biuret)
form
ammonium sulfate suspension
specific activity
≥50 units/mg protein (biuret)
color
white
suitability
suitable for enzyme test
application(s)
life science and biopharma
shipped in
wet ice
storage temp.
2-8°C
Quality Level
Gene Information
Pseudomonas fluorescens ... gdh(533113295)
Application
β-Galactose Dehydrogenase from Pseudomonas fluorescens has been used for competitive inhibition in lectin histochemistry. It has also been used to measure the hydrolysis activity of Haloferax alicantei β-galactosidase on different disaccharides.
Biochem/physiol Actions
β-galactose dehydrogenase catalyzes the oxidation of β-D-galactose to D-galactono-gammalactone.
Physical form
Suspension in 3.2 M (NH4)2SO4, pH approx. 6.0
Other Notes
One unit will convert 1.0 μmole of D-galactose to D-galactonate per min at pH 8.6 at 25 °C.
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Faites votre choix parmi les versions les plus récentes :
Déjà en possession de ce produit ?
Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
Takahiro Mieda et al.
Plant & cell physiology, 45(9), 1271-1279 (2004-10-29)
We have studied the enzymological properties of L-galactose dehydrogenase (l-GalDH), a key enzyme in the biosynthetic pathway of l-ascorbate (AsA) in plants. L-GalDH was purified approximately 560-fold from spinach leaves. The enzyme was a homodimer with a subunit mass of
Optimizing the enzymatic determination of galactose in the culture medium of rat liver and HepG2 cell spheroids.
Jinsheng Xu et al.
Analytical biochemistry, 311(2), 179-181 (2002-12-10)
D Peltzer et al.
Free radical research, 31 Suppl, S181-S185 (2000-02-29)
Green and white variegated leaves of Coleus blumei, Benth. were separated into albino and green sections and used to determine the distribution of vitamin C and L-galactose dehydrogenase activity, an enzyme supposed to be involved in ascorbate metabolism, in heterotrophic
C F Mazitsos et al.
European journal of biochemistry, 269(22), 5391-5405 (2002-11-09)
Protein molecular modelling and ligand docking were employed for the design of anthraquinone galactosyl-biomimetic dye ligands (galactosyl-mimodyes) for the target enzyme galactose dehydrogenase (GaDH). Using appropriate modelling methodology, a GaDH model was build based on a glucose-fructose oxidoreductase (GFO) protein
Stephan Gatzek et al.
The Plant journal : for cell and molecular biology, 30(5), 541-553 (2002-06-06)
l-Galactose dehydrogenase (l-GalDH), a novel enzyme that oxidizes l-Gal to l-galactono-1,4-lactone (l-GalL), has been purified from pea seedlings and cloned from Arabidopsis thaliana. l-GalL is a proposed substrate for ascorbate biosynthesis in plants, therefore the function of l-GalDH in ascorbate
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
Contacter notre Service technique