Ceruloplasmin
Ceruloplasmin, encoded by the CP gene, is a secreted blue copper-binding glycoprotein that binds most of the copper in plasma. It acts as a ferroxidase, oxidising Fe(2+) to Fe(3+), and is also known by the alias AB073614. Browse Assay Genie's current range of Ceruloplasmin research reagents below, or read on for the biology behind the target.
Ceruloplasmin is a multifunctional blue, copper-binding glycoprotein carrying 6-7 copper atoms per molecule. Its best-characterised role is ferroxidase activity: it oxidises Fe(2+) to Fe(3+) without releasing radical oxygen species, and is involved in iron transport across the cell membrane. The resulting ferric iron can be incorporated onto apo-transferrins, and the NCBI Gene summary describes the protein as involved in converting Fe(II)-transferrin to Fe(III)-transferrin.
The copper ions in ceruloplasmin support a broad set of enzymatic activities. The protein catalyses Cu(+) oxidation, promotes the oxidation of biogenic amines such as norepinephrine and serotonin, and provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. It also shows glutathione peroxidase-like activity, removing both hydrogen peroxide and lipid hydroperoxide in the presence of thiols, and inhibits the peroxidase activity of MPO. NO-oxidase and NO2 synthase activities further determine endocrine NO homeostasis.
The CP gene encodes a secreted protein that belongs to the multicopper oxidase family, grouped by HGNC as the multicopper ferroxidase family; the gene was formerly named ceruloplasmin (ferroxidase). Two transcript variants have been described, one protein-coding and one not. Mutations in the gene cause aceruloplasminemia, which results in iron accumulation and tissue damage and is associated with diabetes and neurologic abnormalities. Mouse and rat each have a Cp ortholog.
Ceruloplasmin oxidises ferrous iron for incorporation onto apo-transferrins and is involved in iron transport across the cell membrane.
It binds most of the copper in plasma and catalyses Cu(+) oxidation, making it central to plasma copper biology.
CP mutations cause aceruloplasminemia, with iron accumulation, tissue damage, diabetes and neurologic abnormalities.
Glutathione peroxidase-like, NO-oxidase and NO2 synthase activities link ceruloplasmin to peroxide removal and endocrine NO homeostasis.
Ceruloplasmin is a secreted copper-binding ferroxidase that oxidises Fe(2+) to Fe(3+) without releasing radical oxygen species, supporting iron loading onto apo-transferrins. It also oxidises biogenic amines, shows glutathione peroxidase-like activity, inhibits MPO peroxidase activity and contributes to endocrine NO homeostasis.
The HGNC symbol is CP, the previous name is ceruloplasmin (ferroxidase), and AB073614 is listed as an alias. NCBI Gene reports two transcript variants: one protein-coding and one that is not protein-coding.
Mutations in CP cause aceruloplasminemia, marked by iron accumulation and tissue damage and associated with diabetes and neurologic abnormalities. Orthologs exist in mouse and rat, both named Cp. Check the datasheet of any product for its validated reactivity.
Other proteins whose symbols begin with CP, listed for browsing; they are distinct from ceruloplasmin.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P00450; product specifications from Assay Genie datasheets.