The invention relates to new bispecific antigen binding molecules, comprising (a) a first Fab fragment capable of specific binding to 4-1BB, (b) a second Fab fragment capable of specific binding to a target cell antigen, (c) a third Fab fragment capable of specific binding to 4-1BB, and (d) a Fc domain composed of a first and a second subunit capable of stable association, wherein the Fab fragments (a) and (b) are fused to each other, and to methods of producing these molecules and to methods of using the same.

The present invention relates to novel antigen binding domains and heterodimeric antibodies that bind Fibroblast Activation Protein (FAP).

The present disclosure relates to multispecific binding agents, in particular tetravalent bispecific antibodies, related polynucleotides, vectors, host cells, compositions, and methods of producing the binding agents.

The invention provides antibody-like binding proteins comprising four polypeptide chains that form four antigen binding sites, wherein each pair of polypeptides forming an antibody-like binding protein possesses dual variable domains having a cross-over orientation. The invention also provides methods for making such antigen-like binding proteins.

Binding members for sodium channel Nav1.7 and their use in medicine including for treatment of pain or epilepsy. Binding members comprise a fusion protein containing a Nav1.7-binding peptide, e.g., venom toxin peptide or knottin (“donor diversity scaffold domain”) inserted within an antibody variable domain (“recipient diversity scaffold domain”), and a partner domain (e.g., antibody variable domain), optionally wherein the partner domain enhances specificity of binding to Nav1.7 over other sodium channels.

The present invention concerns antigen binding proteins that bind TL1A, including bispecific antigen binding proteins (e.g., antibodies) to TL1A and TNF-α. Such bispecific antibodies can be in a tetrameric immunoglobulin format, in which one heavy chain-light chain pair of the antibody is directed to TL1A and the other to TNF-α. The bispecific antigen binding proteins may also be comprised in an IgG-scFv fusion, in which a conventional tetrameric antibody directed to one antigen is fused to a pair of single chain Fv units directed to the other. The bispecific antigen binding protein may also be comprised in an IgG-Fab fusion, in which a Fab molecule that binds to one antigen is fused to each heavy chain of a conventional tetrameric antibody directed to the other antigen. The invention further relates to uses of the anti-TL1A binding proteins and anti-TL1A/anti-TNF-α antigen binding proteins, and pharmaceutical formulations thereof.

Disclosed herein are compositions comprising structurally modified DNA encoded antibodies (DMAbs), methods of structurally modifying DMAbs, and methods of using structurally modified DMAbs.

The present invention relates, in part, to bispecific chimeric proteins that find use in various immunotherapies based on various properties, including, for example, a dual immune cell recruitment and immune signal delivery function.

Binding molecules, constructs, pharmaceutical compositions comprising the constructs, and methods of use thereof are presented.

The present invention generally relates to novel bispecific antigen binding molecules for T cell activation and re-direction to specific target cells. In addition, the present invention relates to polynucleotides encoding such bispecific antigen binding molecules, and vectors and host cells comprising such polynucleotides. The invention further relates to methods for producing the bispecific antigen binding molecules of the invention, and to methods of using these bispecific antigen binding molecules in the treatment of disease.