SAE0044
Choline Oxidase from Arthrobacter sp.
recombinant, expressed in E. coli ≥12 units/mg protein
Synonyme(s) :
COD, COX, ChOx, Choline: oxygen 1-oxidoreductase
Se connecter pour consulter les tarifs organisationnels et contractuels.
Sélectionner une taille de conditionnement
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
bacterial (arthrobacter sp.)
recombinant
expressed in E. coli ≥12 units/mg protein
form
powder
specific activity
≥12 units/mg protein
technique(s)
activity assay: suitable
UniProt accession no.
storage temp.
−20°C
Quality Level
General description
Research area: Cell Signaling
Choline oxidase from Arthrobacter sp. is a flavoprotein, which is a member of the glucose–methanol–choline (GMC). The codA gene encodes the choline oxidase enzyme.
Choline oxidase from Arthrobacter sp. is a flavoprotein, which is a member of the glucose–methanol–choline (GMC). The codA gene encodes the choline oxidase enzyme.
Application
Choline oxidase from Arthrobacter sp. has been used in the enzymatic determination of choline in milk using a flow injection analysis (FIA) system with potentiometric detection. It has been used for fluorescent detection of choline released during autotaxin (ATX) activity in conditioned media and plasma.
Biochem/physiol Actions
Choline oxidase from Arthrobacter sp. is a flavoprotein, which is a member of the GMC-oxidoreductase family. The enzyme catalyzes the four-electron-oxidation of choline to glycine betaine via the intermediate betaine aldehyde, in two sequential FAD-dependent reaction steps. The enzyme is useful for enzymatic determination of phosphatidylcholine by coupling with phospholipase D or determination of sphingomyelin by coupling with sphingomyelinase and for cholinesterase activity assays.Choline oxidase (COD) mediating glycine betaine biosynthetic pathway plays a vital role in creating stress resistant transgenic plants.
Preparation Note
It is recommended to reconstitute choline oxidase in phosphate buffer at pH 7.5 supplemented with 10mM EDTA. Reconstituted material can be stored at 2-8 °C for at least 2 weeks.
Tightly closed.Dry. Keep locked up or in an area accessible only to qualified or authorized
persons
persons
Other Notes
One unit will form 1 μmole of H2O2 with oxidation of 1 μmole of choline to betaine aldehyde per min at pH 8.0 at 37 °C. Note: During the conversion of choline to betaine by choline oxidase, 2 μmoles of H2O2 are produced for every μmole of choline.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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.
Transformation of Arabidopsis thaliana with the codA gene for choline oxidase; accumulation of glycinebetaine and enhanced tolerance to salt and cold stress.
Hayashi H, et al.
The Plant Journal, 12(1), 133-142 (1997)
Transformation of Synechococcus with a gene for choline oxidase enhances tolerance to salt stress.
Deshnium P, et al.
Plant Molecular Biology, 29(5), 897-907 (1995)
J L Lima et al.
The Analyst, 125(7), 1281-1284 (2000-09-14)
The development of a FIA system for the determination of total choline content in several types of milk is described. The samples were submitted to hydrochloric acid digestion before injection into the system and passed through an enzymatic reactor containing
Rapid, specific, and sensitive measurements of plasma sphingomyelin and phosphatidylcholine.
Hojjati M.R., and Jiang X.C.
Journal of Lipid Research, 47, 673-676 (2006)
New enzymatic assay of cholinesterase activity
Okabe, H. et al.,
Clinica Chimica Acta; International Journal of Clinical Chemistry, 80, 87-94 (1977)
Contenu apparenté
Instructions
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