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The process of generating a recombinant monoclonal antibody against CASP9 began with the immunization of a rabbit using a synthesized peptide from human CASP9 protein. B cells were subsequently isolated from the immunized rabbit, and RNA was extracted from these B cells. The extracted RNA was reverse-transcribed into cDNA, which was employed as a template to extend CASP9 antibody genes using degenerate primers. These extended CASP9 antibody genes were incorporated into a plasmid vector and transfected into host cells for expression. The CASP9 recombinant monoclonal antibody was then purified from the cell culture supernatant through affinity chromatography and subjected to ELISA, IF, and FC applications. It shows specific reactivity with human CASP9 protein.
CASP9 is a key regulator of apoptosis, serving as the initiator caspase in the intrinsic pathway. Its activation marks the commitment of a cell to undergo programmed cell death, a fundamental process in development, tissue homeostasis, and the elimination of damaged or potentially harmful cells.
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