CLDN18.2-targeting antibody-drug conjugate that binds CLDN18.2 on tumor cells, internalizes, and delivers a cytotoxic payload to kill cancer cells.
Monoclonal antibody targets CLDN18.2 on tumor cells, is internalized, and releases the linked cytotoxic payload MMAE via a cleavable linker; MMAE binds tubulin and inhibits microtubule polymerization, inducing G2/M arrest and apoptosis in CLDN18.2-positive tumor cells.
ADC binds CLDN18.2 on target cells, is internalized, and releases MMAE via a cleavable linker; MMAE inhibits microtubule polymerization, causing G2/M arrest and apoptosis of CLDN18.2-positive cells.
Autologous, ex vivo–expanded tumor-infiltrating lymphocyte (TIL) product composed of polyclonal T cells that recognize patient-specific tumor neoantigens via the TCR and mediate cytotoxicity (perforin/granzyme and IFN-γ).
Autologous, ex vivo–expanded polyclonal TILs that are CRISPR/Cas9-edited to remove immunoregulatory targets; they recognize patient-specific tumor neoantigens via TCR–HLA interactions and kill tumor cells through perforin/granzyme release and IFN-γ–mediated cytotoxicity, enhancing TIL proliferation and function.
Autologous CRISPR-edited TILs recognize the neoantigen–HLA class I complex via their TCR and directly lyse target cells through perforin/granzyme-mediated apoptosis, with IFN-γ/Fas–FasL contributions.
Autologous, ex vivo–expanded tumor-infiltrating lymphocyte (TIL) product composed of polyclonal T cells that recognize patient-specific tumor neoantigens via the TCR and mediate cytotoxicity (perforin/granzyme and IFN-γ).
Autologous, ex vivo–expanded polyclonal TILs that are CRISPR/Cas9-edited to remove immunoregulatory targets; they recognize patient-specific tumor neoantigens via TCR–HLA interactions and kill tumor cells through perforin/granzyme release and IFN-γ–mediated cytotoxicity, enhancing TIL proliferation and function.
TILs recognize the neoantigen–HLA class II complex via their TCR and directly kill the target cell through perforin/granzyme release and IFN-γ–mediated cytotoxicity.
Natural killer cells genetically engineered to express a chimeric antigen receptor using the NKG2D ectodomain, enabling recognition of stress-induced ligands (MICA, MICB, ULBP1–6) on tumor cells and triggering NK activation, degranulation (perforin/granzyme), cytokine release, and death receptor–mediated apoptosis. Administered as two IV infusions on days 2–3 after each chemotherapy cycle with dose escalation.
Genetically engineered NK cells expressing an NKG2D-based chimeric antigen receptor bind stress-induced ligands (MICA, MICB, ULBP1–6) on tumor cells, triggering NK activation with degranulation (perforin/granzyme), cytokine release, and death receptor–mediated apoptosis (e.g., TRAIL/Fas) to kill tumor cells.
NKG2D CAR on NK cells binds MICA on target cells, activating NK cytotoxicity with perforin/granzyme release and death receptor–mediated apoptosis (TRAIL/Fas).
Natural killer cells genetically engineered to express a chimeric antigen receptor using the NKG2D ectodomain, enabling recognition of stress-induced ligands (MICA, MICB, ULBP1–6) on tumor cells and triggering NK activation, degranulation (perforin/granzyme), cytokine release, and death receptor–mediated apoptosis. Administered as two IV infusions on days 2–3 after each chemotherapy cycle with dose escalation.
Genetically engineered NK cells expressing an NKG2D-based chimeric antigen receptor bind stress-induced ligands (MICA, MICB, ULBP1–6) on tumor cells, triggering NK activation with degranulation (perforin/granzyme), cytokine release, and death receptor–mediated apoptosis (e.g., TRAIL/Fas) to kill tumor cells.
NKG2D CAR-NK cells bind MICB on target cells, triggering NK activation with degranulation (perforin/granzyme) and death receptor–mediated apoptosis (e.g., TRAIL/FasL), killing the MICB-expressing cells.