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The synthesis of the NECTIN4 recombinant monoclonal antibody involves a rigorous and precise process to ensure its exceptional quality and specificity. It begins with the isolation of B cells from an immunized animal, using the recombinant human NECTIN4 protein as the immunogen. Total RNA is extracted from these B cells and converted into cDNA through reverse transcription. The NECTIN4 antibody genes are then amplified using specific primers targeting the antibody constant regions and inserted into an expression vector. Through transfection, the vector is introduced into host cells, allowing for the production of the NECTIN4 recombinant monoclonal antibody. After a period of cell culture, the antibody is harvested from the supernatant and subjected to purification using affinity chromatography, resulting in a highly purified form suitable for a wide range of applications. To ensure its reliability and functionality, the antibody undergoes ELISA to validate its specificity in detecting human NECTIN4 protein.
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