An antibody–drug conjugate (Aidixi, RC48) consisting of a humanized anti‑HER2 IgG1 linked via a cleavable linker to the microtubule toxin MMAE; binds HER2, internalizes, releases MMAE to disrupt microtubules, causing mitotic arrest and apoptosis, with potential bystander effect.
Disitamab vedotin is a humanized anti-HER2 IgG1 antibody–drug conjugate linked via a cleavable linker to MMAE. It binds HER2 on tumor cells, is internalized, and releases MMAE intracellularly to inhibit microtubule polymerization, inducing G2/M arrest and apoptosis, with a potential bystander effect on neighboring HER2-low cells.
ADC binds HER2 on target cells, is internalized, and releases MMAE intracellularly to inhibit microtubule polymerization, causing G2/M arrest and apoptosis (with possible bystander effect).
An antibody–drug conjugate consisting of a humanized anti-CD22 monoclonal antibody linked to the cytotoxic agent calicheamicin; it binds CD22 on B-lineage lymphoblasts, is internalized, and releases calicheamicin to induce DNA double-strand breaks and apoptosis.
Humanized anti-CD22 monoclonal antibody linked to calicheamicin; binds CD22 on B-cell lymphoblasts, is internalized, and releases calicheamicin that binds the DNA minor groove, causing double-strand breaks and apoptosis.
ADC binds CD22, is internalized, and releases calicheamicin that binds DNA and induces double‑strand breaks, triggering apoptosis of CD22+ cells.
Bispecific IgG1 monoclonal antibody (MCLA-158) targeting EGFR and LGR5; inhibits EGFR-driven MAPK/PI3K signaling and uses Fc-mediated cytotoxicity/phagocytosis to deplete LGR5+ tumor stem-like cells.
Bispecific IgG1 monoclonal antibody that binds EGFR and LGR5 to block EGFR-driven MAPK/PI3K and LGR5/Wnt signaling, inhibiting tumor proliferation; its Fc domain mediates ADCC/ADCP to deplete LGR5+ cancer stem–like cells.
Petosemtamab binds LGR5 on tumor cells and its IgG1 Fc engages FcγR-expressing effector cells, inducing ADCC (NK cells) and ADCP (macrophages) to deplete LGR5+ cells.
EGFR-targeting monoclonal antibody that inhibits EGFR signaling.
Chimeric IgG1 monoclonal antibody that binds the extracellular domain of EGFR, blocking ligand binding and receptor dimerization/activation, thereby inhibiting downstream signaling (RAS–MAPK, PI3K–AKT) and tumor cell proliferation; may also engage immune effector functions such as ADCC.
Cetuximab binds EGFR on target cells and engages Fcγ receptor–bearing immune cells to mediate antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC); it also blocks EGFR signaling.
Autologous CD19-directed CAR T cells (19-28z CAR with CD28 and CD3ζ signaling domains) engineered to secrete IL-12; includes a truncated EGFR (EGFRt) tag for tracking and potential cetuximab-mediated depletion.
Autologous T cells engineered with an anti-CD19 CAR containing CD28 and CD3zeta signaling domains recognize CD19 on B-cell malignancies, become activated, proliferate, and kill targets via cytotoxic effector mechanisms. The cells are further engineered to secrete IL-12, which enhances Th1/IFN-gamma responses, activates NK cells, and augments cytotoxic T-cell activity to strengthen antitumor immunity. A truncated EGFR (EGFRt) tag enables in vivo tracking and optional depletion of the cells via cetuximab-mediated ADCC as a safety switch.
Anti-CD19 CAR T cells bind CD19 via the CAR (CD28/CD3ζ signaling), activate, and kill the engaged cells through cytotoxic T-cell mechanisms (perforin/granzyme and Fas–FasL). IL-12 secretion enhances this activity.