The present disclosure relates to antibodies directed to CD25 and uses of such antibodies, for example to suppress organ transplant rejection or to treat multiple sclerosis.

The present disclosure provides a method of controlling the Antibody Dependent Cellular Cytotoxicity (ADCC) activity of a glycosylated and afucosylated IgG1 antibody composition. In exemplary embodiments, the method includes (1) determining the ADCC activity of a glycosylated and afucosylated IgG1 antibody composition; and (2) increasing or decreasing the ADCC activity of the IgG1 antibody composition by increasing or decreasing the amount of terminal β-galactose in the afucosylated glycan species at the consensus glycosylation site. Related methods of matching ADCC activity of a reference glycosylated and afucosylated IgG1 antibody composition and methods of engineering a specific target ADCC activity of a glycosylated and afucosylated IgG1 antibody composition are further provided herein.

The invention provides humanized antibodies that specifically bind to BCMA. The antibodies are useful for treatment and diagnoses of various cancers and immune disorders as well as detecting BCMA.

The invention provides anti-CTLA4 binding proteins (e.g., antibodies, bispecific antibodies, and chimeric receptors) and their use in combination with PD-1 signaling agents (e.g., PD-1 inhibitors or PD-L1 inhibitors) for treating and preventing cancer, as well as compositions and kits comprising the anti-CTLA4 binding proteins and PD-1 signaling agents.

The invention relates to binding molecules, such as antibodies, that bind to the chemokine receptor CCR9. More particularly, the invention relates to the treatment of CCR9-mediated diseases or conditions such as inflammatory bowel disease (IBD), and methods for the detection of CCR9, which make use of the binding molecules of the invention.

The invention relates to anti-TNFa antibodies which are engineered to exhibit a pH-sensitive antigen binding. The invention is preferably directed to anti-TNFa antibody adalimumab (Humira®) or biologically active variants and fragments thereof, wherein the original adalimumab antibody or variant or fragment thereof is engineered by modifications of amino acid sequence within the variable regions. Specifically, the invention relates to adalimumab or biologically active variants or fragments thereof, wherein the CDR domains are modified by replacing one or more amino acid residues by histidine residues.

Provided herein are EphA2 antibodies. These EphA2 antibodies bind preferentially to tumor tissue than normal tissue and bind to EphA2. Such antibodies are used in methods of inducing an immune response and methods of inhibiting tumor cell growth. Additionally provided are methods of producing such antibodies.

[Problem] Provided is an anti-human Igβ antibody which crosslinks BCR and FcγRIIb and has an immunosuppressive function more enhanced than that of an antibody in the prior art.

[Means for Solution] An anti-human Igβ antibody comprising a heavy chain variable region comprising CDR1 consisting of the amino acid sequence of amino acid numbers 31 to 35 of SEQ ID NO: 2, CDR2 consisting of the amino acid sequence of amino acid numbers 50 to 65 of SEQ ID NO: 2, and CDR3 consisting of the amino acid sequence of amino acid numbers 98 to 108 of SEQ ID NO: 2, a light chain variable region comprising CDR1 consisting of the amino acid sequence of amino acid numbers 24 to 38 of SEQ ID NO: 4, CDR2 consisting of the amino acid sequence of amino acid numbers 54 to 60 of SEQ ID NO: 4, and CDR3 consisting of the amino acid sequence of amino acid numbers 93 to 101 of SEQ ID NO: 4, and a heavy chain constant region which is a human Igγ1 constant region having amino acid mutations of S239D, H268D, and L328W.

The invention provides anti-OspA antibodies and methods of using the same.

The present application relates to antibody molecules that bind mesothelin (MSLN). The antibody molecules find application in the treatment and diagnosis of diseases and disorders, such as cancer.