Chimeric anti-EGFR monoclonal antibody that inhibits EGFR ligand binding and receptor activation and can engage immune effector functions (ADCC).
Chimeric anti-EGFR monoclonal antibody that binds the extracellular domain of EGFR, blocking ligand binding and receptor activation/dimerization to inhibit downstream RAS-RAF-MEK-ERK signaling and tumor cell proliferation; also mediates immune effector functions via ADCC.
Cetuximab binds EGFR on tumor cells and its Fc engages FcγR-bearing effector cells to mediate ADCC (and can activate complement for CDC), causing lysis/apoptosis; EGFR blockade is antiproliferative.
Type II glycoengineered anti-CD20 monoclonal antibody with enhanced ADCC and direct cell death activity, used to deplete CD20+ B cells.
A type II glycoengineered humanized IgG1 anti-CD20 monoclonal antibody that binds CD20 on B cells and, through enhanced affinity for Fc gamma RIIIa (CD16), mediates strong antibody-dependent cellular cytotoxicity and induces direct, caspase-independent cell death, leading to depletion of CD20-positive B cells (with relatively less complement activation than type I anti-CD20 mAbs).
Binds CD20 on B cells and recruits FcγRIIIa+ effector cells (e.g., NK cells) to trigger strong ADCC; also induces direct, caspase‑independent cell death (with relatively less complement-mediated lysis).
Autologous genetically modified T cells engineered ex vivo to express a chimeric antigen receptor targeting a myeloma-associated surface antigen; administered as a CAR T cell infusion to drive antigen-dependent T-cell activation, proliferation, cytokine release, and cytotoxic killing of malignant plasma cells.
Autologous T cells are genetically engineered ex vivo to express a chimeric antigen receptor recognizing a myeloma-associated surface antigen. Upon antigen binding, CAR signaling (CD3ζ with costimulation) drives antigen-dependent activation, proliferation, cytokine release, and perforin/granzyme-mediated cytotoxic killing of malignant plasma cells in an MHC-independent manner, with in vivo expansion and persistence enabling sustained antitumor activity.
CAR T cells bind the myeloma-associated surface antigen and, upon CAR signaling, kill target cells via perforin/granzyme-mediated cytotoxicity (and death receptor pathways) in an MHC-independent manner.
Human IgG1κ monoclonal antibody targeting CD38 on clonal plasma cells; mediates complement-dependent cytotoxicity, antibody-dependent cellular cytotoxicity/phagocytosis, and apoptosis, and modulates immune cells to reduce pathogenic monoclonal immunoglobulin/light-chain production.
Human IgG1κ monoclonal antibody targeting CD38 on clonal plasma cells; induces CDC, ADCC, and ADCP and can trigger apoptosis. Also depletes CD38+ immunosuppressive cells (e.g., Tregs, Bregs, MDSCs), reducing pathogenic monoclonal immunoglobulin/light-chain production.
Anti-CD38 IgG1 binds CD38 and triggers complement-dependent cytotoxicity, Fc-mediated ADCC by NK cells, antibody-dependent phagocytosis, and can induce apoptosis of CD38+ cells.
Felzartamab is a human IgG1 monoclonal antibody targeting CD38. It binds CD38 and depletes CD38-positive cells via Fc-mediated effector functions (ADCC, ADCP, and possibly complement). In this study, two formulations (T by I-Mab Biopharma and R by Patheon Italia) of the same drug were compared after a single 8 mg/kg IV dose for PK, safety, tolerability, and immunogenicity.
Human IgG1 monoclonal antibody targeting CD38; binds CD38 on plasma cells and other CD38+ immune cells and depletes them via Fc-mediated effector functions (ADCC, ADCP, and complement), resulting in reduction of CD38-expressing cells.
IgG1 antibody binds CD38 on target cells; Fc region engages Fcγ receptors on NK cells/macrophages to mediate ADCC/ADCP and activates complement (CDC), leading to depletion of CD38+ cells.