Ceruloplasmin [9031-37-2]
16-16-030518
Protein IDP00450
Product group Proteins / Signaling Molecules
Overview
- SupplierAthens Research
- Product NameCeruloplasmin [9031-37-2]
- Delivery Days Customer9
- Applications SupplierInflammation, Cancer, Cardiovascular Disease, Protein Chemistry, Copper Transport, Wilson's Disease, In Vitro Diagostic, Iron Oxidation
- CAS Number9031-37-2
- CertificationResearch Use Only
- Estimated Purity≥95% by SDS-PAGE
- Protein IDP00450
- Protein NameCeruloplasmin
- Scientific DescriptionCeruloplasmin (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.
- Shelf life instructionmore then 1 year
- SourceSource human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
- Storage Instruction≤ -20° C
- UNSPSC41116100
References
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- Sharma, P., et al., (2019), 'Biallelic HEPHL1 variants impair ferroxidase activity and cause an abnormal hair phenotype', PLoS Genet 15(5): e1008143.Read this paper
- Sarpong-Kumankomah, S., et al. (2019), 'Identification of a haptoglobin-hemoglobin complex in human blood plasma', Journal of Inorganic Biochemistry 201: pp 110802.Read this paper
- 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.Read this paper
- Kirsipuu, T., et al., (2020), 'Copper(II)-binding equilibria in human blood', Scientific Reports., 10: 5686.Read this paper