Abstract: The present disclosure provides isolated monoclonal anti-CD3epsilon antibodies or antigen-binding fragments thereof comprising one or more heavy chain CDR sequences selected from the group consisting of: SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, and 47, and/or one or more kappa light chain CDR sequences selected from the group consisting of: SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46 and 48, isolated polynucleotides encoding the same, pharmaceutical compositions comprising the same, and the use thereof.

Abstract: The present disclosure provides isolated monoclonal anti-CD3epsilon antibodies or antigen-binding fragments thereof comprising one or more heavy chain CDR sequences selected from the group consisting of: SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, and 47, and/or one or more kappa light chain CDR sequences selected from the group consisting of: SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46 and 48, isolated polynucleotides encoding the same, pharmaceutical compositions comprising the same, and the use thereof.

Abstract: Provided are bispecific antibodies against CD3 and EGFR, the nucleic acid molecules encoding the antibodies, expression vectors and host cells used for the expression of the antibodies. The antibodies provide a potent agent for the treatment of CD3-related and/or EGFR-related diseases via modulating immune functions.

Abstract: Provided are anti-CD47 antibodies, the nucleic acid molecules encoding the anti-CD47 antibodies, expression vectors and host cells used for the expression of anti-CD47 antibodies. Provided are methods for validating the function of antibodies. The antibodies provide a potent agent for the treatment of cancers via modulating immune functions.

Abstract: The present disclosure provides isolated monoclonal anti-CD3epsilon antibodies or antigen-binding fragments thereof comprising one or more heavy chain CDR sequences selected from the group consisting of: SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, and 47, and/or one or more kappa light chain CDR sequences selected from the group consisting of: SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46 and 48, isolated polynucleotides encoding the same, pharmaceutical compositions comprising the same, and the use thereof.

Abstract: A bispecific anti-CD3×CD19 polypeptide complex that contains a first antigen-binding moiety of the polypeptide complex and a second antigen-binding moiety, methods of producing the bispecific anti-CD3×CD19 polypeptide complex, methods of treating disease or disorder using the bispecific anti-CD3×CD19 polypeptide complex, polynucleotides encoding the bispecific anti-CD3×CD19 polypeptide complex, vectors and host cells containing said polynucleotides, and compositions and pharmaceutical compositions comprising the bispecific anti-CD3×CD19 polypeptide complex are provided.

Abstract: The present disclosure provides a bispecific anti-CD3×CD20 polypeptide complex that contains a first antigen-binding moiety of the polypeptide complex and a second antigen-binding moiety, methods of producing the bispecific anti-CD3×CD20 polypeptide complex, methods of treating disease or disorder using the bispecific anti-CD3×CD20 polypeptide complex, polynucleotides encoding the bispecific anti-CD3×CD20 polypeptide complex, vectors and host cells containing said polynucleotides, and compositions and pharmaceutical compositions comprising the bispecific anti-CD3×CD20 polypeptide complex.

Abstract: Provided are a bispecific antibody comprising a first antigen-binding site that specifically binds to CD3 and a second antigen-binding site that specifically binds to an antigen different from CD3. It also provides the method for producing the bispecific antibody, and the use thereof.

Abstract: The present disclosure provides isolated monoclonal anti-CD3epsilon antibodies or antigen-binding fragments thereof comprising one or more heavy chain CDR sequences selected from the group consisting of: SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, and 47, and/or one or more kappa light chain CDR sequences selected from the group consisting of: SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46 and 48, isolated polynucleotides encoding the same, pharmaceutical compositions comprising the same, and the use thereof.

Abstract: A bispecific anti-CD3×CD19 polypeptide complex that contains a first antigen-binding moiety of the polypeptide complex and a second antigen-binding moiety, methods of producing the bispecific anti-CD3×CD19 polypeptide complex, methods of treating disease or disorder using the bispecific anti-CD3×CD19 polypeptide complex, polynucleotides encoding the bispecific anti-CD3×CD19 polypeptide complex, vectors and host cells containing said polynucleotides, and compositions and pharmaceutical compositions comprising the bispecific anti-CD3×CD19 polypeptide complex are provided.

Abstract: A method and device for controlling switching of a virtual navigation bar, wherein the method includes: a terminal device receiving a command for displaying or hiding a virtual navigation bar from a user; after receiving the command for displaying hiding a virtual navigation bar from the user, the terminal device determining display objects of a display content in a window, re-rendering and refreshing the display content in the current window, wherein, upon receiving the command for displaying a virtual navigation bar from the user, the display objects of the display content in the window contain a display object of the virtual navigation bar; and upon receiving the command for hiding a virtual navigation bar from the user, the display objects of the display content in the window do not contain the display object of the virtual navigation bar.

Abstract: The present invention features antibodies referred to herein as “MAb50-4” and “MAb184-10”, and polypeptides that compete with MAb50-4 and MAb184-10 for binding to CYP2D6. MAb50-4 can be produced by ATCC No. PTA-3489, while MAb184-10 can be produced by ATCC No. PTA-1999.

Abstract: Particularly sensitive techniques for the detection of P. carinii in clinical samples are disclosed. These techniques relate to the PCR amplification and/or detection of human-P. carinii major surface glycoprotein (MSG) gene sequences. Also disclosed are seven novel genes encoding human-P. carinii MSG, and the proteins encoded for by these genes. These genes provide proof that human-P. carinii MSG is encoded for by a highly conserved gene family, and that the corresponding proteins have a very highly conserved region of about 100 amino acids near their C-terminal end. This highly conserved carboxy-terminal region has a significantly different sequence than that found in rat-derived MSG.

Abstract: The present invention features antibodies referred to herein as “MAb50-4” and “MAb184-10”, and polypeptides that compete with MAb50-4 and MAb184-10 for binding to CYP2D6. MAb50-4 can be produced by ATCC No. PTA-3489, while MAb184-10 can be produced by ATCC No. PTA-1999.

Abstract: Particularly sensitive techniques for the detection of P. carinii in clinical samples are disclosed. These techniques relate to the PCR amplification and/or detection of human-P. carinii major surface glycoprotein (MSG) gene sequences. Also disclosed are seven novel genes encoding human-P. carinii MSG, and the proteins encoded for by these genes. These genes provide proof that human-P. carinii MSG is encoded for by a highly conserved gene family, and that the conesponding proteins have a very highly conserved region of about 100 amino acids near their C-terminal end. This highly conserved carboxy-terminal region has a significantly different sequence than that found in rat-derived MSG.