Ceruloplasmin humain, poudre lyophilisée, oxidase 20-75 unités/mg protéine

Code: c4519-100un D2-231

Non disponible en dehors du Royaume-Uni et de l'Irlande

Analysis Note

Protein determined by biuret

Biochem/physiol Actions

Ceruloplasmin (Cp), the principal carrier of copper in plasma, is thought to b...


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Non disponible en dehors du Royaume-Uni et de l'Irlande

Analysis Note

Protein determined by biuret

Biochem/physiol Actions

Ceruloplasmin (Cp), the principal carrier of copper in plasma, is thought to be involved in oxidative modification of lipoproteins and participate in the acute phase reaction to stress. Cp is an effective antioxidant for a variety of radicals and has a potent peroxidase activity to decompose hydrogen peroxide in the presence of reduced glutathione. It inhibits the peroxidase activity of myeloperoxidase in a concentration-dependent manner and shows selective binding to myeloperoxidase in vitro. This suggests that ceruloplasmin may participate in the clearance and inactivation of myeloperoxidase in vivo. At physiological (micromolar) concentrations it was found to inhibit relaxation of rabbit aorta induced by endothelium-dependent agonists like acetylcholine or ADP. However, it was found ineffective toward vasodilation due to direct stimulation of smooth muscle cells by nitroglycerin. Cp plays an essential role in iron homeostasis, regulating the efflux of iron from macrophages and the oxidation of Fe2+ to Fe3+. Cp deficiency leads to neurodegenerative disorders, possibly by starving neurons of iron.

Physical form

Pale blue powder containing sodium chloride and sodium acetate

Unit Definition

One unit will cause a ΔA550 of 0.01 per min using N,N-dimethyl-p-phenylenediamine as substrate at pH 5.5 and 37 °C, in a 7 mL reaction volume.

compositionProtein, ~30%
copper content1.0-2.5 µg/mg protein
formlyophilized powder
Gene Informationhuman ... CP(1356)
mol wt~135 kDa
oxidase activity20-75 units/mg protein
Quality Level200
storage temp.−20°C
UniProt accession no.P00450
Cas Number9031-37-2
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