Abstract: Disclosed is a humanized 4-1BB monoclonal antibody, an antigen-binding fragment thereof, a pharmaceutical composition and a medical use thereof. The monoclonal antibody comprises CDR1 with the amino acid sequence shown in SEQ ID NO: 1 or SEQ ID NO: 4, CDR2 with the amino acid sequence shown in SEQ ID NO: 2 or SEQ ID NO: 5, CDR3 with the amino acid sequence shown in SEQ ID NO: 3, CDR1? with the amino acid sequence shown in SEQ ID NO: 6, CDR2? with the amino acid sequence shown in SEQ ID NO: 7, CDR3? with the amino acid sequence shown in SEQ ID NO: 8. The monoclonal antibody binds to human 4-1BB with high affinity and specificity, leads to a significant increase in T cell proliferation and TNF-? production, and enhances and stimulates human 4-1BB-mediated immune response.

Abstract: Disclosed is a bispecific antibody with dual Her2 binding sites, comprising (a) an anti-CD3 antigen-binding fragment Fab, having a light chain variable region VL, a light chain constant region CL, a heavy chain variable region VH and a heavy chain constant region CH1; (b) an anti-Her2 single domain antigen-binding fragment VHH1, linked to the C-terminus of the CL of the Fab and can bind to a first Her2 epitope; and (c) an anti-Her2 single domain antigen-binding fragment VHH2, linked to the C-terminus of CH1 of the Fab and can bind to a second Her2 epitope; the first Her2 epitope and the second Her2 epitope are non-overlapping epitopes of Her2. The bispecific antibody has a killing effect on Her2 tumors with an IHC score of +1, and is effective on trastuzumab-resistant tumors.

Abstract: Disclosed is a PEGylated bispecific antibody, comprising (a) an antigen-binding fragment (Fab), which has a light chain variable region (VL) and a light chain constant region (CL), a heavy chain Variable region (VH) and a part of the heavy chain constant region (CH1); (b) a single domain antigen binding fragment (VHH) fused to the C-terminus of the part of the heavy chain constant region (CH1) of the antigen binding fragment (Fab), and (c) Polyethylene glycol (PEG) fused to the C-terminus of the light chain constant region (CL) of the antigen-binding fragment (Fab). The PEGylated S-Fab (PEG-S-Fab) retained the binding specificity to both tumor cells and T cells. PEG-S-Fab enhanced the plasma stability and had a 12-fold increased half-life of S-Fab. PEG-S-Fab also had more potent tumor inhibiting efficacy in xenograft mouse model. Those data suggest that PEGylation can be an effective approach to enhance anti-tumor properties of bispecific antibodies.

Abstract: The present invention provides an anti-VEGF monoclonal antibody, which has the variable region of heavy chain comprising the amino acid sequences of SEQ ID NO:1, SEQ ID NO:2 and SEQ ID NO:3, and/or the variable region of light chain comprising the amino acid sequences of SEQ ID NO:4, SEQ ID NO:5 and SEQ ID NO:6. The antibody can be produced by the cell line with the preservation number of CGMCC NO. 3233. The invention also provides the use of said antibody for the manufacture of medicaments for the treatment of a disease that is relevant to VEGF, wherein further provided are pharmaceutical composition, agents, kits and chips comprising said antibody, as well as the cell line with the preservation number of CGMCC NO. 3233.

Abstract: The present invention provides an anti-VEGF monoclonal antibody, which has the variable region of heavy chain comprising the amino acid sequences of SEQ ID NO. 1, SEQ ID NO. 2 and SEQ ID NO. 3, and/or the variable region of light chain comprising the amino acid sequences of SEQ ID NO. 4, SEQ ID NO. 5 and SEQ ID NO. 6. The antibody can be produced by the cell line with the preservation number of CGMCC NO. 3233. The invention also provides the use of said antibody for the manufacture of medicaments for the treatment of a disease that is relevant to VEGF, wherein further provided are pharmaceutical composition, agents, kits and chips comprising said antibody, as well as the cell line with the preservation number of CGMCC NO. 3233.