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The process of producing the EGFR recombinant monoclonal antibody begins by acquiring the EGFR antibody genes. These genes are then introduced into appropriate host cells, which are cultured for synthesizing EGFR antibodies. This method offers several advantages, including a substantial enhancement in the purity and stability of the resulting EGFR recombinant monoclonal antibodies, as well as an increase in their affinity and specificity. Following synthesis, the EGFR recombinant monoclonal antibody undergoes purification through affinity chromatography. Subsequently, it undergoes comprehensive testing via various assays, including ELISA, IHC, and FC. This antibody exclusively recognizes the human EGFR protein.
EGFR is a vital cell surface receptor involved in regulating various aspects of cell growth, differentiation, and survival. Its dysregulation can contribute to cancer development, making it an important target for cancer therapy. Additionally, EGFR signaling plays a role in tissue repair, development, and immune modulation.
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