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Ceruloplasmin (human plasma)

Serum copper transport protein
ALX-200-089-M001 1 mg 414.00 USD
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Serum copper transport and iron-oxidizing protein. Expressed in plasma at concentrations of 1-5µM. Contains six copper centers and is known to oxidize amines in a process coupled to the reduction of molecular oxygen. Has ferroxidase activity that is responsible for the oxidation of ferrous iron to its ferric form, which is necessary for efficient iron efflux from the cell (e.g. during hypoxia). Has previously been considered a target for nitric oxide (NO) and an inhibitor of endothelial nitric oxide synthase (eNOS/NOS III). Catalyzes S-nitrosothiol formation in cell culture media. Is a NO oxidase and nitrite synthase that determines endocrine NO homeostasis.

Product Details

Alternative Name:Ferroxidase
Source:Isolated from human plasma.
MI:14: 2006
UniProt ID:P00450
Formulation:Lyophilized from 50mM potassium phosphate, pH 6.8, containing 100mM potassium chloride, 20mM ε-aminocaproic acid and 5mM EDTA.
Purity:≥95% (SDS-PAGE)
Purity Detail:Plasma has been tested negative for HBsAg and for antibodies to HIV and HCV.
Reconstitution:Reconstitute with distilled water.
Shipping:Blue Ice
Long Term Storage:-20°C
Regulatory Status:RUO - Research Use Only

Product Literature References

Ceruloplasmin replacement therapy ameliorates neurological symptoms in a preclinical model of aceruloplasminemia: A. Zanardi, et al.; EMBO Mol. Med. 10, 91 (2018), Abstract; Full Text
Identification of Ceruloplasmin as a Gene that Affects Susceptibility to Glomerulonephritis Through Macrophage Function: T.D. Chen, et al.; Genetics 206, 1139 (2017), Abstract; Full Text
Serological immune response against ADAM10 pro-domain is associated with favourable prognosis in stage III colorectal cancer patients: S.M. Alverez-Fernandez, et al.; Oncotarget 7, 80059 (2016), Abstract; Full Text
Ceruloplasmin functional changes in Parkinson’s disease-cerebrospinal fluid: M. Barbariga, et al.; Mol. Neurodegener. 10, 59 (2015), Application(s): Ceruloplasmin in CSFs and immunoprecipitation, Abstract; Full Text
Oxidation-induced structural changes of ceruloplasmin foster NGR-motifs deamidation that promote integrin binding and signalling: M. Barbariga, et al.; J. Biol. Chem. 289, 3736 (2014), Application(s): Use in cell culture, Abstract; Full Text
Epitope specificity determines pathogenicity and detectability in ANCA-associated vasculitis: A.J. Roth, et al.; J. Clin. Invest. 123, 1773 (2013), Application(s): Control for mass spectrometry analysis, Abstract; Full Text
Ceruloplasmin is a NO oxidase and nitrite synthase that determines endocrine NO homeostasis: S. Shiva, et al.; Nat. Chem. Biol. 2, 486 (2006), Abstract;
Does oxidative stress change ceruloplasmin from a protective to a vasculopathic factor?: N. Shukla, et al.; Atherosclerosis 187, 238 (2006), Abstract;
Role of ceruloplasmin in macrophage iron efflux during hypoxia: J. Sarkar, et al.; J. Biol. Chem. 278, 44018 (2003), Abstract; Full Text
Inhibition of endothelial nitric-oxide synthase by ceruloplasmin: A. Bianchini, et al.; J. Biol. Chem. 274, 20265 (1999), Abstract; Full Text
The reactions of copper proteins with nitric oxide: J. Torres & M.T. Wilson; Biochim. Biophys. Acta 1411, 310 (1999), Abstract;
Antioxidant protection against organic and inorganic oxygen radicals by normal human plasma: the important primary role for iron-binding and iron-oxidising proteins: J.M. Gutteridge & G.J. Quinlan; Biochim. Biophys. Acta 1156, 144 (1993), Abstract;
Ceruloplasmin inhibits carbonyl formation in endogenous cell proteins: J.A. Krsek-Staples & R.O. Webster; Free Radic. Biol. Med. 14, 115 (1993), Abstract;
Copper transport: an overview: E.D. Harris; Proc. Soc. Exp. Biol. Med. 196, 130 (1991), Abstract;
The reaction of nitric oxide with ceruloplasmin: R. Wever, et al.; Biochim. Biophys. Acta 302, 236 (1973), Abstract;

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