Ceruloplasmin is a ferroxidase combining more than 95% copper atoms in plasma that plays roles in copper transport and regulates iron homeostasis. In this study, a full-length cDNA of ceruloplasmin was cloned from channel catfish Ictalurus punctatus. The cDNA of ceruloplasmin has a length of 4 110 bp, composed of a 25 bp 5′ UTR, an 860 bp 3′ UTR and a 3 225 bp ORF, encoding a polypeptide of 1,074 amino acids. Alignments showed that catfish ceruloplasmin was conserved among others. Quantitative real-time PCR was conducted to detect expression profiles of ceruloplasmin in normal tissues and four tissues (liver, headkidney, intestine and spleen) after infection by different pathogens: Edwardsiella tarda, Streptococcus iniae, Aeromonas hydrophila, and channel catfish Hemorrhage Reovirus (CCRV). The expression profile in liver was the highest in normal tissues. S. iniae induced the expression of ceruloplasmin to the highest extent, and CCRV virus to the lowest extent. These results provide a basis for further research aimed at exploring the precise immune-related molecular mechanism of ceruloplasmin in channel catfish.