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The synthesis of the ROR1 recombinant monoclonal antibody involves a meticulous process to ensure its exceptional quality and specificity. It begins with the isolation of B cells from an immunized animal, where the recombinant human ROR1 protein is used as the immunogen. Total RNA is extracted from these B cells and converted into cDNA through reverse transcription. The ROR1 antibody genes are then amplified using specific primers designed for the antibody constant regions and inserted into an expression vector. Following transfection, the vector is introduced into host cells, enabling the production of the ROR1 recombinant monoclonal antibody. After cell culture, the antibody is harvested from the supernatant and purified using affinity chromatography, resulting in a highly purified form suitable for diverse applications. Rigorous characterization assays, including ELISA and FC analysis, are performed to validate the antibody's specificity and functionality in detecting human ROR1 protein.
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