Anti-Ceruloplasmin/CP Antibody Picoband® Fluoro647 Conjugated

Ceruloplasmin  (or  caeruloplasmin) is a  ferroxidase  enzyme  that in humans is encoded by the  CP  gene. It is mapped to 3q23-q25. 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.

E. coli-derived human Ceruloplasmin recombinant protein (Position: K20-M259) . Human Ceruloplasmin shares 80.8% and 79.6% amino acid (aa) sequence identity with mouse and rat Ceruloplasmin, respectively.

Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe (2+) to Fe (3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu (2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity) . .

1. Koschinsky ML, Funk WD, van Oost BA, MacGillivray RT (Jul 1986) .Complete cDNA sequence of human preceruloplasmin. Proceedings of the National Academy of Sciences of the United States of America 83 (14) : 5086–90. 2. Royle NJ, Irwin DM, Koschinsky ML, MacGillivray RT, Hamerton JL (May 1987) . Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively. Somatic Cell and Molecular Genetics 13 (3) : 285–92. 3. Takahashi N, Ortel TL, Putnam FW (Jan 1984) . Single-chain structure of human ceruloplasmin: the complete amino acid sequence of the whole molecule. Proceedings of the National Academy of Sciences of the United States of America 81 (2) : 390–4.