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The protein encoded by CP is a metalloprotein that binds most of the copper in plasma and is involved in the peroxidation of Fe(II)transferrin to Fe(III) transferrin. Additionally we are shipping Ceruloplasmin (Ferroxidase) Antibodies (117) and Ceruloplasmin (Ferroxidase) Kits (101) and many more products for this protein.
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In D-galactosamine-sensitized mice CP+Cu(II) increased the LPS (show TLR4 Proteins)-induced lethality from 54 to 100%, while administration of antibodies against MIF (show MIF Proteins) prevented the lethal effect. The enhancement by CP+Cu(II) of the pro-inflammatory signal of MIF (show MIF Proteins) is discussed
mice with mutation of Cp and Heph (show HEPH Proteins), iron accumulates in glia, while neurons have low iron levels. Both neurons and glia degenerate and mice become ataxic unless given an iron chelator.
Data (including data from studies in knockout mice) suggest that ceruloplasmin and hephaestin (show HEPH Proteins) play distinct roles in regulation of gene expression in various regions of the brain and are involved in iron homeostasis.
Evidence supports a regulatory role of both proteins (Ceruloplasmin (CP) and beta-amyloid protein precursor (APP (show APP Proteins))) in defence against iron-induced oxidative damage after TBI (show TBPL1 Proteins), which presents as a tractable therapeutic target.
Genetic interactions between Cp, Mon1a (show MON1A Proteins), and the Slc40a1 (show SLC40A1 Proteins) locus are involved in iron metabolism.
ceruloplasmin should provide a protective shield against inadvertent oxidant production by myeloperoxidase (show MPO Proteins) during inflammation
The mouse ceruloplasmin gene has been mapped to chromosome 3.
Data found an increase in ceruloplasmin levels in the plasma of Npc1 (show NPC1 Proteins) -/- mice compared to Npc1 (show NPC1 Proteins) +/+ mice, and this increase was statistically significant (*p < 0.05).
Cp and Heph (show HEPH Proteins) are necessary for iron export from the retina but are not essential for iron import into the retina.
pathological cerebrospinal fluid's environment of Parkinson's disease patients promoted the same modifications in the exogenously added ceruloplasmin
PON-1 (show PON1 Proteins) and ferroxidase activities in older patients with mild cognitive impairment, late onset Alzheimer's disease or vascular dementia
we have through bioinformatic screening identified ceruloplasmin as a novel adipokine with increased expression in adipose tissue of obese subjects as well as in cells from obesity-associated cancers.
brain microvascular endothelial cell -secreted cytokine activity increases the gene expression of neighboring C6 glioma CP, which reciprocally acts on basolateral BMVEC ferroportin (show SLC40A1 Proteins) to enhance brain iron import
High ceruloplasmin levels are associated with preeclampsia.
A reduced serum FeOx activity, which can potentially lead to a rise in oxidative stress-induced (show SQSTM1 Proteins) biomolecular damage, seems to be a shared condition in inflammatory disorders of the central nervous system including MS.
This review describes the main role of ceruloplasmin in iron turnover is oxidizing Fe2+ into Fe3+, a process which is essential for iron binding to transferrin (show Tf Proteins) (the main iron-transporting protein), as well as to ferritin (show FTL Proteins) (the main iron-storage protein)
ceruloplasmin and hepcidin (show HAMP Proteins) differentially regulate iron efflux from brain microvascular endothelial cells
The core-fucosylation ratio of ceruloplasmin increases significantly in alcohol-related hepatocellular carcinoma.
In CKD patients, increased serum ceruloplasmin, a regulator of nitric oxide activity, is associated with increased risk of long-term adverse cardiovascular events, even after multivariable model adjustment for traditional clinical/biologic risk factors.
The protein encoded by this gene is a metalloprotein that binds most of the copper in plasma and is involved in the peroxidation of Fe(II)transferrin to Fe(III) transferrin. Mutations in this gene cause aceruloplasminemia, which results in iron accumulation and tissue damage, and is associated with diabetes and neurologic abnormalities. Two transcript variants, one protein-coding and the other not protein-coding, have been found for this gene.
, hypothetical protein
, ceruloplasmin (ferroxidase)