Humanized IgG1 bispecific antibody targeting GPRC5D on myeloma/plasma cells and CD3 on T cells; administered subcutaneously to engage T cells and redirect cytotoxicity against GPRC5D-expressing malignant plasma cells in relapsed/refractory multiple myeloma.
Humanized IgG1 bispecific antibody that simultaneously binds GPRC5D on myeloma/plasma cells and CD3 on T cells, bringing T cells into proximity with tumor cells to form an immune synapse and activate T-cell mediated cytotoxicity against GPRC5D-expressing malignant plasma cells.
Bispecific antibody binds GPRC5D on tumor cells and CD3 on T cells, forming an immune synapse that activates T-cell cytotoxicity (perforin/granzyme-mediated killing) of GPRC5D-expressing cells.
CRISPR-edited, allogeneic anti-BCMA CAR T-cell therapy engineered from donor T cells to target BCMA on malignant plasma cells and induce T-cell–mediated cytotoxicity.
CRISPR-edited, allogeneic T cells engineered with an anti-BCMA chimeric antigen receptor bind BCMA on malignant plasma cells, triggering T‑cell activation and cytotoxic killing. TRAC knockout removes endogenous TCR to reduce graft‑versus‑host disease, while B2M knockout and insertion of a B2M–HLA‑E fusion minimize host T- and NK‑cell rejection, enhancing persistence and antitumor activity.
Anti-BCMA CAR T cells recognize BCMA on target cells and induce T-cell–mediated killing via perforin/granzyme release and death-receptor pathways.
Allogeneic, genetically modified natural killer cells engineered to express an anti-BCMA chimeric antigen receptor that recognizes BCMA (TNFRSF17) on malignant plasma cells and triggers NK-mediated cytotoxicity and cytokine release to kill tumor cells.
Allogeneic NK cells engineered to express an anti-BCMA chimeric antigen receptor bind BCMA (TNFRSF17) on malignant plasma cells, activating NK and CAR signaling to induce perforin/granzyme-mediated cytotoxicity and cytokine release, resulting in tumor cell apoptosis.
Anti-BCMA CAR-engineered NK cells bind BCMA on target cells, activate NK/CAR signaling, and kill through immune-synapse formation with perforin/granzyme-mediated cytolysis (and death-receptor pathways), inducing apoptosis.
An investigational HER2-targeted antibody-drug conjugate (ADC). The monoclonal antibody binds HER2 (including low-HER2 expressers), is internalized, and releases a cytotoxic payload to induce tumor cell death and suppress proliferation; targets HER2/ERBB signaling pathways.
HER2-targeted monoclonal antibody (trastuzumab-based) binds HER2, including low-expressing cells, is internalized, and after linker cleavage releases a camptothecin-derived topoisomerase I–inhibiting payload that induces DNA damage, leading to cell-cycle arrest and apoptosis and suppression of HER2-driven tumor proliferation.
The HER2-targeted ADC binds HER2 on tumor cells, is internalized, and releases a camptothecin-derived topoisomerase I inhibitor that induces DNA damage, leading to cell-cycle arrest and apoptosis.
Anti-CD20 monoclonal antibody given once on Cycle 1 Day 1.
Obinutuzumab is a glycoengineered, humanized type II anti-CD20 IgG1 monoclonal antibody that binds CD20 on B cells and depletes malignant B cells primarily via enhanced Fc-mediated effector functions (increased binding to FcγRIIIa leading to potent antibody‑dependent cellular cytotoxicity and phagocytosis) and by inducing direct, caspase‑independent cell death.
Anti‑CD20 antibody binds CD20 on B cells and kills them via FcγRIIIa‑mediated ADCC and phagocytosis, and also induces direct, caspase‑independent cell death (with some complement involvement).