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The development of the DLL3 recombinant monoclonal antibody involves a meticulous step-by-step process to ensure its exceptional quality and specificity. Initially, B cells are isolated from the spleen of an immunized animal, with the recombinant human DLL3 protein used as the immunogen. The RNA extracted from the B cells is converted into cDNA through reverse transcription. The DLL3 antibody genes are then amplified using specific primers designed for the antibody constant regions and inserted into an expression vector. This vector is subsequently transfected into host cells, enabling the production of the DLL3 recombinant monoclonal antibody. After a period of cell culture, the antibody is harvested from the cell culture supernatant and purified using affinity chromatography, resulting in a highly purified form suitable for various applications. Rigorous characterization assays, including ELISA and FC analysis, are performed to validate the antibody's specificity and functionality in detecting human DLL3 protein.
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