Abstract
The significance of expression systems for quickly creating enough numbers of therapeutic monoclonal antibodies to make them available to patients has been heightened in recent years due to advances in the creation of genetically modified monoclonal antibodies. The conventional method for making recombinant proteins involves first cloning the desired gene into an expression vector, and then testing how well it expresses itself in cells. For cellular expression and perpetuation, a plasmid containing the chosen genes is then cloned. The most significant and lucrative subset of biopharmaceuticals is monoclonal antibodies (mAbs). To temporarily produce an anti-CD20 monoclonal antibody in mammalian cells, this work created and assessed an antiCD20 mAb expression construct. The gene fragment was transferred to the expression vector after the vector (pcDNA3.1+) was synthesised by sequentially cloning the Light Chain (LC) and Heavy Chain (HC). We co-transfected HEK 293 cells and then examined the cell culture supernatant for antibody clone expression. Using this technology to transiently express the whole monoclonal antibody in mammalian cells was a breeze, and our findings prove it.
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