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The synthesis of the RPS6KB1 recombinant monoclonal antibody involves a meticulous and well-defined process to ensure its exceptional quality and specificity. Initially, B cells are isolated from the spleen of an immunized animal, with the synthesized peptide derived from human P70 S6 Kinase alpha serving as the immunogen. RNA is then extracted from the B cells and converted into cDNA through reverse transcription. The RPS6KB1 antibody genes are amplified using specific primers targeting the antibody constant regions and inserted into an expression vector. This vector is subsequently introduced into host cells via transfection, enabling the production of the RPS6KB1 recombinant monoclonal antibody. Following a period of cell culture, the antibody is harvested from the cell culture supernatant and subjected to a meticulous purification process utilizing affinity chromatography. This ensures the obtainment of a highly purified form of the RPS6KB1 recombinant monoclonal antibody suitable for various applications. Rigorous characterization assays, including ELISA and IF analysis, are performed to validate the antibody's specificity and functionality in detecting human RPS6KB1 protein. The rigorous production process guarantees the development of a reliable and effective RPS6KB1 recombinant monoclonal antibody, serving as an invaluable tool in diverse research related to RPS6KB1.
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