Human Ceruloplasmin
Native whole molecule
Produktdetails
Synonyms
CP, Cuproxidase ceruloplasmin, Ferroxidase ceruloplasmin, Glutathione peroxidase ceruloplasmin, Glutathione-dependent peroxiredoxin ceruloplasmin
Description of Human Ceruloplasmin
Human Ceruloplasmin is a 132 kDa protein. Ceruloplasmin (Cp), a ferroxidase belonging to the multi-copper oxidase family, serves as the primary copper transport protein in plasma, binding 95% of circulating copper. Beyond copper homeostasis, Cp exhibits critical roles in iron metabolism by oxidizing Fe²⁺ to Fe³⁺ for transferrin-mediated transport, lipid regulation, and antioxidant defense. As an acute-phase reactant, Cp levels rise during inflammation, infection, trauma, and pregnancy due to estrogen-induced hepatic synthesis. Reduced Cp levels hallmark Wilson’s disease (impaired copper ATPase) and aceruloplasminemia (genetic ferroxidase loss), causing copper deposition in tissues and neurodegenerative iron accumulation, respectively. Elevated Cp correlates with rheumatoid arthritis severity (as an acute-phase marker), liver cirrhosis progression, and cardiovascular risk via prooxidant LDL oxidation in atherosclerotic plaques. Cp also predicts tumor aggressiveness in breast, lung, and ovarian cancers. Cp serves as a biomarker for Wilson’s disease screening and preeclampsia monitoring. In chronic hepatitis B, Cp combined with GGT forms a non-invasive model for liver fibrosis staging. Therapeutic strategies targeting Cp’s ferroxidase activity or copper-binding sites are under exploration for neurodegenerative and oncological disorders.
Source
Human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests
Storage
For long term, store Human Ceruloplasmin at ≤ -20°C.
Applications
Inflammation, Cancer, Cardiovascular Disease, Protein Chemistry, Copper Transport, Wilson's Disease, In Vitro Diagostic, Iron Oxidation.
Citations/Publications
Shao, S., et al., (2017), 'A non-cytotoxic dendrimer with innate and potent anticancer and anti-metastatic activities', Nature Biomedical Engineering , 1: pp 745–757. Available at: DOI: 10.1038/s41551-017-0130-9
Sharma, P., et al., (2019), 'Biallelic HEPHL1 variants impair ferroxidase activity and cause an abnormal hair phenotype', PLoS Genet 15(5): e1008143. Available at: https://doi.org/10.1371/journal.pgen.1008143
Sarpong-Kumankomah, S., et al. (2019), 'Identification of a haptoglobin-hemoglobin complex in human blood plasma', Journal of Inorganic Biochemistry 201: pp 110802. Available at: https://doi.org/10.1016/j.jinorgbio.2019.110802
Hermann, G., et al., (2016), 'In vivo synthesized 34S enriched amino acid standards for species specific isotope dilution of proteins', J. Anal. At. Spectrom., 31: pp 1830. Available at: DOI: 10.1039/c6ja00039h
Kirsipuu, T., et al., (2020), 'Copper(II)-binding equilibria in human blood', Scientific Reports., 10: 5686. Available at: https://doi.org/10.1038/s41598-020-62560-4
NCBI: https://www.ncbi.nlm.nih.gov/protein/P00450/
Shipped with ice packs
Gel Scan of Human Ceruloplasmin
Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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Payment Methods
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