An anti-CD38 antibody–drug conjugate composed of a human anti-CD38 (A2) monoclonal antibody covalently linked to a duostatin (auristatin-like) tubulin inhibitor payload; after binding CD38 on multiple myeloma cells and internalization, it releases the cytotoxic payload to disrupt microtubules causing mitotic arrest and apoptosis, and may also mediate ADCC/CDC.
STI-6129 is an anti‑CD38 monoclonal antibody conjugated to a duostatin/MMAF tubulin‑inhibiting payload. After binding CD38 on myeloma cells and internalization, it releases the cytotoxic payload that inhibits tubulin polymerization, causing G2/M arrest and apoptosis; Fc-mediated ADCC/CDC may also contribute.
Anti‑CD38 ADC binds CD38, is internalized, and releases an MMAF/auristatin payload that inhibits tubulin polymerization, causing G2/M arrest and apoptosis; Fc interactions can also induce ADCC/CDC.
Anti‑CD20 monoclonal antibody that depletes malignant B cells via antibody‑dependent cellular cytotoxicity, complement‑dependent cytotoxicity, and induction of apoptosis.
Chimeric anti-CD20 monoclonal antibody that binds CD20 on B cells and depletes CD20-positive malignant and normal B cells via antibody-dependent cellular cytotoxicity, complement-dependent cytotoxicity, and induction of apoptosis.
Rituximab binds CD20 on B cells and triggers antibody-dependent cellular cytotoxicity via FcγR+ effector cells, complement-dependent cytotoxicity (C1q/MAC), and can induce apoptosis of CD20+ cells.
Chimeric anti-CD20 monoclonal antibody that depletes B cells via antibody-dependent cellular cytotoxicity, complement-dependent cytotoxicity, and apoptosis.
Chimeric anti-CD20 monoclonal antibody that binds CD20 on B lymphocytes and depletes them via antibody-dependent cellular cytotoxicity, complement-dependent cytotoxicity, and apoptosis.
Rituximab binds CD20 on B cells, opsonizing them for Fcγ receptor–mediated ADCC by NK/macrophages, activates complement (CDC) to lyse cells, and can trigger apoptosis via CD20 crosslinking.
An EGFR-targeted antibody–drug conjugate that delivers the microtubule-disrupting payload MMAE; after binding EGFR and internalization, MMAE causes G2/M arrest and apoptosis.
EGFR-targeted antibody-drug conjugate (becotatug vedotin) linked to MMAE. After binding EGFR on tumor cells and internalization, MMAE is released to bind tubulin and inhibit polymerization, leading to microtubule disruption, G2/M cell-cycle arrest, and apoptosis in EGFR-expressing cells.
EGFR-targeted ADC binds EGFR, is internalized, and releases MMAE that inhibits tubulin polymerization, leading to microtubule disruption, G2/M arrest, and apoptosis of EGFR-expressing cells.
Chimeric anti-EGFR monoclonal antibody that blocks ligand binding and receptor activation and mediates antibody-dependent cellular cytotoxicity (ADCC).
Cetuximab is a chimeric monoclonal antibody against EGFR that blocks ligand binding and prevents receptor activation and dimerization, suppressing downstream signaling (e.g., RAS/RAF/MEK/ERK, PI3K/AKT) to inhibit tumor cell proliferation; it also mediates antibody‑dependent cellular cytotoxicity (ADCC) against EGFR-expressing cells.
Cetuximab binds EGFR on target cells and engages immune effectors via its Fc to induce antibody‑dependent cellular cytotoxicity (ADCC) (and potentially complement-mediated lysis), killing EGFR+ cells; it also blocks EGFR signaling (antiproliferative).