The development of the NUF2 recombinant monoclonal antibody involves a rigorous and standardized process to ensure its quality and specificity. B cells are initially isolated from an immunized animal, with the synthesized peptide derived from human NUF2 used as the immunogen. The extracted B cells are then subjected to total RNA extraction and cDNA synthesis through reverse transcription. The NUF2 antibody genes are amplified using specific primers targeting the antibody constant regions and inserted into an expression vector. This vector is subsequently transfected into host cells to enable the production of the NUF2 recombinant monoclonal antibody. Following cell culture, the antibody is harvested from the supernatant and purified using affinity chromatography, resulting in a highly purified preparation. Extensive characterization assays, including ELISA and WB analysis, are performed to validate the antibody's specificity and functionality, ensuring its accurate binding to human NUF2 protein.
