Chimeric IgG1 anti-EGFR monoclonal antibody that blocks ligand binding to EGFR, inhibiting MAPK/ERK and PI3K/AKT signaling and potentially mediating ADCC.
Cetuximab is a chimeric IgG1 monoclonal antibody that binds the extracellular domain of EGFR, blocking ligand binding and receptor dimerization, thereby inhibiting downstream MAPK/ERK and PI3K/AKT signaling to reduce tumor cell proliferation and survival; its Fc region can also trigger antibody-dependent cellular cytotoxicity (ADCC).
Cetuximab coats EGFR-expressing cells and its IgG1 Fc engages Fcγ receptors on effector cells (e.g., NK cells) to trigger ADCC (and some CDC), leading to target-cell lysis; EGFR blockade is mainly antiproliferative.
An antibody–drug conjugate (ADC) also known as iza-bren, izalontamab brengitecan (BMS-986507). The antibody targets a tumor-associated surface antigen, is internalized, and releases a 'gitecan' topoisomerase I inhibitor payload that induces DNA damage and tumor cell death.
Dual-targeting anti-EGFR/anti-HER3 antibody–drug conjugate. The antibody binds EGFR (HER1) and HER3 (ErbB3) on tumor cells, is internalized, and releases a 'gitecan' topoisomerase I inhibitor payload that induces DNA damage and tumor cell death.
The ADC binds EGFR on tumor cells, is internalized, and releases a topoisomerase I inhibitor (gitecan) payload that induces DNA damage, killing EGFR-expressing cells.
An antibody–drug conjugate (ADC) also known as iza-bren, izalontamab brengitecan (BMS-986507). The antibody targets a tumor-associated surface antigen, is internalized, and releases a 'gitecan' topoisomerase I inhibitor payload that induces DNA damage and tumor cell death.
Dual-targeting anti-EGFR/anti-HER3 antibody–drug conjugate. The antibody binds EGFR (HER1) and HER3 (ErbB3) on tumor cells, is internalized, and releases a 'gitecan' topoisomerase I inhibitor payload that induces DNA damage and tumor cell death.
The ADC binds HER3 on tumor cells, is internalized, and releases a topoisomerase I inhibitor (“gitecan”) that causes DNA damage leading to tumor cell death.
Autologous genetically modified T cells expressing a chimeric antigen receptor targeting CD70, incorporating CD3ζ and costimulatory domains to activate, expand, secrete cytokines, and kill CD70-positive tumor cells after IV infusion.
Autologous T lymphocytes genetically engineered to express a chimeric antigen receptor targeting CD70. Upon binding CD70 on tumor cells, the CAR’s CD3ζ and costimulatory domains activate the T cells, driving proliferation, cytokine release, and cytotoxic killing of CD70-positive cells via perforin/granzyme and death-receptor pathways.
CAR-T cells recognize CD70 via the CAR, become activated (CD3ζ/costimulatory signaling), and kill CD70+ cells through perforin/granzyme release and death-receptor (Fas/TRAIL)–mediated apoptosis.
Antigen-specific T cells expanded ex vivo and reinfused to recognize tumor peptides on MHC class I via the TCR, mediating cytotoxicity through perforin/granzyme release and IFN-gamma-mediated effects.
Autologous antigen-specific CTLs expanded ex vivo are reinfused to recognize tumor peptides presented on MHC class I via their endogenous TCR, inducing tumor-cell killing via perforin/granzyme release and death-receptor pathways (FasL/TRAIL), along with IFN-γ secretion to enhance antitumor immune responses.
Antigen-specific CTLs recognize the tumor peptide presented by HLA-A via their TCR and kill the presenting cells through perforin/granzyme-mediated cytolysis and death-receptor (FasL/TRAIL)–induced apoptosis.