Anti-CD38 IgG1 monoclonal antibody that targets CD38 on T-ALL blasts and mediates complement-dependent cytotoxicity, antibody-dependent cellular cytotoxicity/phagocytosis, apoptosis, and immunomodulation.
Human IgG1κ anti-CD38 monoclonal antibody that binds CD38 on malignant cells, triggering complement-dependent cytotoxicity (CDC), antibody-dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP), and direct apoptosis; also depletes CD38+ immunosuppressive cells, leading to immunomodulation.
Daratumumab binds CD38 on target cells and induces complement-dependent cytotoxicity (CDC), Fc-mediated ADCC by NK cells, ADCP by macrophages, and can trigger apoptosis upon crosslinking.
Autologous T lymphocytes genetically engineered to express a chimeric antigen receptor targeting CD30 (TNFRSF8) for TCR-independent recognition and killing of CD30-positive Hodgkin/Reed–Sternberg cells.
Autologous T lymphocytes engineered to express a chimeric antigen receptor that binds CD30 (TNFRSF8) on Hodgkin/Reed–Sternberg cells, enabling TCR-independent recognition and activation through CD3ζ and co-stimulatory domains, resulting in T-cell expansion, cytokine release, and perforin/granzyme-mediated lysis of CD30-positive tumor cells.
CAR T cells bind CD30 on target cells and, upon activation via CD3ζ/co-stimulatory domains, kill CD30+ cells by perforin/granzyme-mediated cytolysis and Fas–FasL apoptosis.
An antibody–drug conjugate comprising a humanized anti–Trop-2 IgG linked to SN-38 (active metabolite of irinotecan), delivering a topoisomerase I inhibitor to Trop-2–expressing tumor cells to induce DNA damage and apoptosis.
Humanized anti–Trop-2 IgG linked to SN-38 (active irinotecan metabolite). The antibody binds Trop-2 on tumor cells, is internalized, and releases SN-38 after cleavage. SN-38 inhibits topoisomerase I by stabilizing Topo I–DNA complexes, causing DNA strand breaks, blocking replication, and inducing apoptosis, with potential bystander cytotoxicity.
ADC binds TROP2 on tumor cells, is internalized, and releases SN-38 intracellularly; SN-38 inhibits topoisomerase I, causing DNA breaks and apoptosis (with possible bystander killing).
Autologous anti-CD4 chimeric antigen receptor T-cell therapy: patient T cells are lentivirally transduced to express an anti-CD4 scFv (derived from humanized mAb ibalizumab) linked to a third-generation CAR with CD28 and 4-1BB co-stimulatory domains and a CD3ζ activation domain; administered as a single IV dose after lymphodepleting chemotherapy to target and eliminate CD4+ leukemic blasts.
Autologous T cells are lentivirally transduced to express an anti-CD4 scFv-based third-generation CAR (CD28 and 4-1BB costimulatory domains with CD3zeta signaling). After lymphodepletion and IV infusion, the CAR T cells bind CD4 on leukemic blasts, triggering activation, expansion, cytokine release, and perforin/granzyme-mediated cytotoxic killing of CD4+ cells. Expected on-target effect includes depletion of normal CD4 T cells (T-cell aplasia).
Anti-CD4 CAR T cells bind CD4 on target cells, become activated, and kill via perforin/granzyme-mediated cytolysis (and possibly Fas–FasL apoptosis), leading to depletion of CD4+ cells.
Autologous, genetically engineered TCR-T cell therapy expressing an HLA-A*11:01–restricted T cell receptor specific for the KRAS G12D neoantigen; administered after lymphodepletion with a single IV infusion to recognize KRAS G12D peptides on tumor HLA-A*11:01, expand (with low-dose IL-2 support), and mediate cytotoxic killing of tumor cells in advanced solid tumors.
Autologous T cells are engineered to express an HLA-A*11:01–restricted TCR that recognizes the KRAS G12D neoantigen. Following lymphodepletion and IV infusion (with low-dose IL-2 support), the cells bind KRAS G12D peptides presented on tumor HLA-A*11:01, activate, expand, and mediate MHC-restricted cytotoxic killing of tumor cells.
Engineered TCR-T cells recognize KRAS G12D peptide presented by HLA-A*11:01 on tumor cells and directly induce cytotoxic T-lymphocyte killing (perforin/granzyme-mediated apoptosis, Fas–FasL).