Abstract: Herein is reported the use of a binding assay of a bivalent, bispecific antibody that has the smaller kD value (dissociation constant) for the interaction with its antigen for the immobilization of the bivalent, bispecific antibody to a solid surface for the determination of the biological activity of the bivalent, bispecific antibody.

Abstract: Herein is reported a method for determining the binding affinity of the binding sites of a bivalent full length antibody of the human IgG1 subclass to a homo-multimeric antigen comprising the steps of i) incubating a mixture comprising the antibody and a polypeptide that is derived from lysine-gingipain of Porphyromonas gingivalis at a pH of from pH 7.5 to pH 8.5, in the presence of a reducing agent, at a temperature of from 30° C. to 42° C., for time of from 10 min. to 240 min. to cleave the antibody into Fabs and Fc-region, and ii) determining the binding affinity of the Fabs of the antibody for its antigen using a surface plasmon resonance method by directly applying the incubated reaction mixture obtained in the previous step in the surface plasmon resonance method and therewith determining the binding affinity of the binding sites of the bivalent full length antibody of the human IgG1 subclass.

Abstract: Herein is reported a method for determining the binding interaction with a multimeric antigen of an antibody of the human IgG1 subclass that has at least two binding sites specifically binding to the antigen comprising the steps of 1) determining the binding affinity of the antibody for the multimeric antigen, and 2) incubating a mixture comprising the antibody and a polypeptide that is derived from lysine-gingipain of Porphyromonas gingivalis under conditions and for a time sufficient to cleave the antibody into Fabs and Fc-region, and determining the binding affinity of the Fabs of the antibody for the multimeric, whereby the binding affinity of the antibody to the multimeric antigen to be affinity-driven if the binding affinity determined in both steps are comparable and to be avidity-driven if the binding affinity determined in both steps are different.

Abstract: The present invention relates to bispecific anti-CCL2 antibodies binding to two different epitopes on human CCL2, pharmaceutical compositions thereof, their manufacture, and use as medicaments for the treatment of cancers, inflammatory, autoimmune and ophthalmologic diseases.

Abstract: The present invention relates to multispecific antibodies that bind to HLA-G ant to a T cell activating antigen, their preparation, formulations and methods of using the same.

Abstract: The present invention relates to anti-HLA-G antibodies and methods of using the same.

Abstract: The invention provides humanized anti-human Tau(pS422) antibodies and methods of using the same.

Abstract: The present invention relates to anti-VEGF antibodies and methods of their production and their use.

Abstract: The present invention relates to methods for improving anti-VEGF antibodies in order to provide or improve antibodies that preferentially inhibit binding to VEGF to VEGF-R2 rather than VEGF binding to VEGF-R1; and antibodies provided by said methods.

Abstract: The invention provides humanized anti-human Tau(pS422) antibodies and methods of using the same.

Abstract: Herein are reported novel bispecific antibodies that specifically bind to two different antigens selected from the group consisting of human ANG2, human VEGF, human IL-1beta and human PDGF-B.

Abstract: The present invention relates to anti-VEGF/anti-IL-1beta antibodies and methods of using the same.

Abstract: Herein are reported anti-ANG2 antibodies. A specific anti-ANG2 antibody comprises (a) a HVR-H1 comprising the amino acid sequence of SEQ ID NO: 20, (b) a HVR-H2 comprising the amino acid sequence of SEQ ID NO: 21, and (c) a HVR-H3 comprising the amino acid sequence of SEQ ID NO: 23.

Abstract: Herein is reported a method for determining the binding of an antibody, which comprises a first binding site specifically binding to a first antigen and a second binding site specifically binding to a second antigen, to said first and said second antigen, wherein the method comprises the steps of capturing the antibody on a solid phase using a capture reagent specifically binding to a constant domain of the antibody, incubating the captured antibody with the first or the second antigen to form a captured antibody-antigen complex and determining a first binding signal, either i) incubating the captured antibody-antigen complex with the antigen not used for the formation of the captured antibody-antigen complex to form a captured antibody-antigen-antigen complex and determining a second binding signal, or ii) regenerating the surface, capturing the antibody on a solid phase using a capture reagent specifically binding to a constant domain of the antibody, incubating the captured antibody with the antigen not us

Abstract: Bispecific tetravalent antibodies against IL-17 and TNFa, useful in therapy, e.g. the treatment of rheumatoid arthritis and other autoimmune diseases and/or to reduce pathological inflammatory conditions.

Abstract: The present invention relates to bispecific antibodies comprising at least one antigen binding site specific for DR5 and at least one antigen binding site specific for FAP, antibodies specific for DR5, methods for their production, pharmaceutical compositions containing said antibodies, and uses thereof.

Abstract: Herein is reported a method for determining the binding affinity of the binding sites of a bivalent full length antibody of the human IgG1 subclass to a homo-multimeric antigen comprising the steps of i) incubating a mixture comprising the antibody and a polypeptide that is derived from lysine-gingipain of porphyromonas gingivalis at a pH of from pH 7.5 to pH 8.5, in the presence of a reducing agent, at a temperature of from 30° C. to 42° C., for time of from 10 min. to 240 min. to cleave the antibody into Fabs and Fc-region, and ii) determining the binding affinity of the Fabs of the antibody for its antigen using a surface plasmon resonance method by directly applying the incubated reaction mixture obtained in the previous step in the surface plasmon resonance method and therewith determining the binding affinity of the binding sites of the bivalent full length antibody of the human IgG1 subclass.

Abstract: Herein is reported a method for determining the binding interaction with a multimeric antigen of an antibody of the human IgG1 subclass that has at least two binding sites specifically binding to the antigen comprising the steps of 1) determining the binding affinity of the antibody for the multimeric antigen, and 2) incubating a mixture comprising the antibody and a polypeptide that is derived from lysine-gingipain of porphyromonas gingivalis under conditions and for a time sufficient to cleave the antibody into Fabs and Fc-region, and determining the binding affinity of the Fabs of the antibody for the multimeric, whereby the binding affinity of the antibody to the multimeric antigen to be affinity-driven if the binding affinity determined in both steps are comparable and to be avidity-driven if the binding affinity determined in both steps are different.

Abstract: Herein are reported anti-PDGF-B antibodies and their use in ophthalmology.

Abstract: The present invention relates to bispecific antibodies comprising at least one antigen binding site specific for DR5 and at least one antigen binding site specific for FAP, antibodies specific for DR5, methods for their production, pharmaceutical compositions containing said antibodies, and uses thereof.