10 results about "Complement-dependent cytotoxicity" patented technology

Disclosed is a polypeptide dimeric protein containing two monomers, each of which contains an extracellular domain (FcεRIa-ECD) of an alpha subunit of an IgE Fc receptor. The dimeric protein has advantages that an excellent binding ability to IgE is exhibited as compared with a conventional therapeutic agent containing an anti-IgE antibody, and less other side effects are exhibited due to lack of ADCC and CDC functions. Thus, the dimeric protein can be applied to a medical product for treating or preventing an IgE-mediated allergic disease.

The present disclosure provides multiple anti-hCD20 mAbs as well as humanization of antibodies. The antibodies described herein are chicken-derived and exhibit significantly enhanced B-cell-specific antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC) potency as well as improved depletion of B lymphoma cells in vivo relative to Rituximab.

NEO-201 is a humanized IgG1 monoclonal antibody (mAb) that is highly reactive against the majority of tumor tissues from a number of different cancer tumors, including colon, pancreatic, gastric, lung, breast and uterine cancers, but the majority of normal tissues are not recognized by such antibodies. Functional assays reveal that NEO-201 is capable of mediating both antibody dependent cytotoxicity (ADCC) and complement dependent cytotoxicity (CDC) against tumor cells. Furthermore, the growth of human pancreatic xenograft tumors in vivo is greatly weakened by using NEO-201 alone and in combination with human peripheral blood mononuclear cells (PBMCs) that are effector cell sources for ADCC. In-vivo biological distribution research in mice carrying human tumor xenografts reveals that NEO-201 is preferentially accumulated in tumors rather than organ tissues. Single dose toxicity studies in non-human primates demonstrate the safety and tolerance of NEO-201 because the transient reduction of circulating neutrophils is the sole associated side effect observed.

This article describes antibodies or antigen-binding fragments that specifically bind to GPRC5D. Additionally, it includes monovalent antibodies or antigen-binding fragments that specifically bind to GPRC5D. The Fc regions of these antibodies contain K248E and T437R mutations (referred to as “RE mutations”) according to the EU numbering system. The described antibodies, when expressed in host cells lacking fucosylation capacity, exhibit enhanced antibody-dependent cytotoxicity (ADCC) and enhanced complement-dependent cytotoxicity (CDC).

To provide an antibody against CD38, a preparation method therefor and the use thereof.SOLUTION: The present disclosure relates to an antibody that binds to the CD38 protein or an antigen-binding portion thereof, a preparation method therefor and the use thereof. The antibody can bind to human CD38 with high affinity, has an inhibitory effect on the CD38 enzyme, has a CDC, ADCC, and / or ADCP killing activity with regard to different tumor cells, and has an anti-tumor function. Moreover, the antibody does not cause red blood cell lysis.SELECTED DRAWING: Figure 4-1

Herein are antibodies or antigen-binding fragments specifically binding to GPRC5D. Additionally, monovalent antibodies or antigen-binding fragments specifically binding to GPRC5D are also included. The Fc region of these antibodies contains K248E and T437R mutations (designated as “RE mutations”) per the EU numbering system. The described antibodies, expressed in host cells that lack fucosylation capabilities, exhibit enhanced antibody-dependent cellular cytotoxicity (ADCC) and enhanced complement-dependent cytotoxicity (CDC).

Described herein are polypeptides comprising variant Fc domains and related antibodies. The variant Fc domains provide stable Fc:Fc interactions when the polypeptides, one or more antibodies, bind to their target(s), one or more antigens, on the surface of a cell, thus providing improved complement-dependent cytotoxicity (CDC).

The application belongs to the technical field of biological medicine, and discloses an anti-BCMA antibody or antigen binding fragment thereof, and a preparation method and application thereof. The amino acid sequences of CDR1-3 of the heavy chain variable region of the anti-BCMA antibody or antigen binding fragment thereof are respectively shown as SEQ ID NO:2-4, and the amino acid sequences of CDR1-3 of the light chain variable region are respectively shown as SEQ ID NO:6-8. The anti-BCMA antibody or antigen binding fragment thereof has excellent affinity to BCMA protein, especially the extracellular segment, can specifically recognize and combine the BCMA protein well, can be applied as a detection antibody of the BCMA protein to realize non-diagnostic purpose detection of BCMA. Meanwhile, the anti-BCMA antibody or antigen binding fragment thereof can realize effective killing of tumor cells overexpressing BCMA, such as pfeiffer cells, through complement-dependent cytotoxicity, and the cell killing rate is as high as 99%, and can be used as an inhibitor of abnormal bone marrow cells overexpressing BCMA protein, is an extremely potential active component for treating hematological malignancies, and has a good application prospect.

Herein are methods of treating multiple myeloma in a subject comprising administering GPRC5D antibodies with enhanced antibody-dependent cellular cytotoxicity (ADCC) and enhanced complement-dependent cytotoxicity (CDC). The antibodies described in the methods are afucosylated and comprise K248E and T437R mutations (designated as "RE mutations") per the EU numbering system.

A monoclonal antibody of IgM isotype which specifically binds to the antigen glypican-1 (GPC1) in vitro, ex vivo and in vivo, is able to induce complement dependent cytotoxicity and reduce GPC1-expressing tumor masses in vivo. A nucleic acid construct and a transformed host cell are suitable for use in a method of recombinantly producing the anti-GPC1 monoclonal antibody and in diagnostic and therapeutic methods.