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The creation of the CCR4 recombinant monoclonal antibody involves a meticulous process aimed at ensuring its exceptional quality and specificity. Initially, B cells are isolated from the spleen of an immunized animal using the recombinant human CCR4 protein as the immunogen. RNA is then extracted from the B cells and converted into cDNA through reverse transcription. The CCR4 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, enabling the production of the CCR4 recombinant monoclonal antibody. After a period of cell culture, the antibody is harvested from the cell culture supernatant and subjected to purification using affinity chromatography, resulting in a highly purified form suitable for various applications. Stringent characterization assays, including ELISA and FC analysis, are conducted to validate the antibody's specificity and functionality in detecting human CCR4 protein. The rigorous production process ensures the generation of a reliable and effective CCR4 recombinant monoclonal antibody, which plays a crucial role in a wide range of CCR4-related research.
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