In order to prepare the recombinant TAB1 protein of Ctenopharyngodon idellus (CiTAB1) and its specific antibodies, firstly, the full-length CiTAB1 gene was amplified using the cDNA of grass carp head kidney as template in the study. Meanwhile, the recombinant cloning plasmid pMD19-T-CiTAB1 and expression plasmid pET-32a-CiTAB1 were successively constructed. Subsequently, the recombinant expression plasmid was induced by 0.5 mmol·L^-1 IPTG for 12 h at 37 °C, and the recombinant CiTAB1 protein (rCiTAB1) expressed as the form of inclusion body was obtained. Secondly, denaturation of rCiTAB1 protein was carried out by using three different methods, respectively. It was found that rCiTAB1 protein treated by gradient urea denaturation after washing was purer compared with the direct high concentration urea denaturation and urea denaturation after washing, and the protein concentration reached 2 mg·mL^-1 after dialysis renaturation. Finally, rCiTAB1 protein mixed with white oil adjuvant and immunopotentiator, respectively, and then stirred at room temperature for 1.5 h to obtain a stable immunogen. New Zealand white rabbits were immunized with the above-mentioned immunogen three times for preparing rabbit anti-CiTAB1 antibodies. The titers of specific antibodies in the serum at 33 days post-vaccination were 1∶1 048 576 and 1∶16 detected by indirect ELISA and immunoagar bidirectional diffusion test, respectively. A specific band with a molecular weight of approximately 72 kDa was detected by Western blot, indicating that the antibody could specifically recognize the rCiTAB1 protein. The results of this study provide the basis for the further reseach on the function of CiTAB1 protein.