A human IgG1κ monoclonal antibody administered intravenously with FcRn-enhanced half-life that binds the “a” determinant on hepatitis B surface antigen (HBsAg). It neutralizes HBV virions and subviral particles, forms immune complexes to accelerate antigen clearance, engages Fcγ receptor–mediated effector functions (e.g., ADCC, phagocytosis), and lowers circulating HBsAg to mitigate T-cell exhaustion and potentially restore adaptive immune responses.
Human IgG1κ monoclonal antibody with FcRn-enhanced half-life that binds the “a” determinant of hepatitis B surface antigen (HBsAg). It neutralizes HBV virions and subviral particles and forms immune complexes that accelerate antigen clearance, while engaging Fcγ receptors to drive ADCC and phagocytosis. By lowering circulating HBsAg, it may reduce T-cell exhaustion and help restore HBV-specific adaptive immune responses.
The IgG1 mAb binds HBsAg on HBV-infected hepatocytes and engages Fcγ receptors on NK cells/macrophages to trigger ADCC (and potentially ADCP), leading to killing of HBsAg-expressing cells; it also neutralizes free virions.
Allogeneic, off-the-shelf adoptive T-cell therapy composed of donor CMV-specific T lymphocytes expanded ex vivo, stimulated with CMV pp65 peptide and selected via IFN-γ capture; exerts HLA-restricted, antigen-specific TCR recognition with CD4+ helper and CD8+ cytotoxic activity against CMV-infected cells.
Allogeneic donor-derived CMV-specific T lymphocytes expanded ex vivo and selected via IFN-γ capture after CMV pp65 peptide stimulation. These cells use their native, HLA-restricted TCRs to recognize CMV antigens on infected host cells; CD8+ T cells mediate perforin/granzyme cytotoxicity and CD4+ T cells provide helper functions, restoring antigen-specific antiviral immunity.
CMV-specific donor T cells recognize the pp65 peptide–MHC I complex via their native, HLA-restricted TCRs and kill infected cells through CD8+ perforin/granzyme-mediated cytotoxicity (with CD4+ helper support).
Investigational anticancer agent from Hengrui; mechanism/target not specified in the registry. Studied in combination with rituximab-containing chemotherapy.
Monoclonal antibody targeting CD79b on B-cell lymphomas delivers a topoisomerase I inhibitor payload. After binding and internalization, the payload is released to inhibit DNA topoisomerase I, blocking DNA replication and inducing cell cycle arrest and apoptosis in CD79b-expressing tumor cells.
ADC binds CD79b on B cells, is internalized, and releases a topoisomerase I inhibitor that blocks DNA replication, causing DNA damage, cell cycle arrest, and apoptosis of CD79b-expressing cells.
Anti-CD20 monoclonal antibody that depletes CD20+ B cells via ADCC, complement-dependent cytotoxicity, and induction of apoptosis; component of the R-chemotherapy regimen.
Chimeric anti-CD20 monoclonal antibody that binds CD20 on pre-B and mature B cells and depletes CD20+ cells via antibody-dependent cellular cytotoxicity (ADCC), complement-dependent cytotoxicity (CDC), and induction of apoptosis.
Binding to CD20 triggers Fc-mediated ADCC by immune effector cells, complement-dependent cytotoxicity, and can induce apoptosis of CD20+ cells.
Chimeric anti-CD20 monoclonal antibody that depletes CD20+ B cells via antibody-dependent cellular cytotoxicity, complement-dependent cytotoxicity, and apoptosis.
Chimeric anti-CD20 monoclonal antibody that binds CD20 on B cells and depletes CD20+ cells via antibody-dependent cellular cytotoxicity, complement-dependent cytotoxicity, and induction of apoptosis.
Rituximab binds CD20 on B cells and recruits immune effectors via its Fc to mediate ADCC (e.g., NK cells/macrophages), activates complement for CDC/lysis, and can trigger apoptosis upon CD20 cross-linking.