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B lymphocytes were generated by immunizing an animal with a synthetic peptide derived from human EGFR and then fused with myeloma cells to generate hybridomas. The variable light and heavy domains of the resulting EGFR antibody-producing hybridomas were sequenced to construct a vector for recombinant production. The EGFR monoclonal antibody gene-containing vector was then transfected into cells for cultivation, and the resulting derived from human EGFR recombinant monoclonal antibody was purified using affinity chromatography from the cell culture supernatant. The purified antibody was found to be highly specific for human EGFR protein, as confirmed by ELISA, WB, and IHC assays.
The EGFR protein is a transmembrane receptor protein that plays a key role in the regulation of cell growth and division. When activated by ligands, such as EGF or TGF-alpha, EGFR initiates a signaling cascade that leads to the activation of downstream effectors, such as MAPK and PI3K, which ultimately result in changes in gene expression, cell proliferation, differentiation, and survival. Abnormal activation of EGFR signaling has been implicated in various human diseases, including cancer.
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