Abstract: This disclosure relates to methods of generating antibody libraries, antibody libraries produced using such methods, and variant antibodies. Presently, methods of improving antibody binding (affinity maturation assays) require the screening of vast libraries of antibody variants (often >1010) to identify a small fraction of variants with improved characteristics. The present invention involves taking the nucleotide sequence of the framework and complementarity determining region of a target antibody and identifying motifs which would be recognised by deamination somatic hypermutation enzymes. A small library of variants is then created which incorporate one or more of these mutations. It was found that a relatively high proportion of the variants have an increased affinity. The technique of the present invention was demonstrated on the trastuzumab and Cathepsin S antibodies, and the variants produced are also claimed.

Abstract: The present invention aims to provide a humanized antibody or an antigen-binding fragment thereof having stable physical property, superior in tumor accumulation, and capable of binding to mucin subtype 5AC. The above-mentioned problem is solved by the present invention that provides a humanized antibody or an antigen-binding fragment thereof having a heavy chain variable region consisting of the amino acid sequence shown in SEQ ID NO: 1-4 or a mutated amino acid sequence thereof, and a light chain variable region consisting of the amino acid sequence shown in SEQ ID NO: 5-8 or a mutated amino acid sequence thereof, and capable of binding to mucin subtype 5AC.

Abstract: This disclosure relates to methods of generating antibody libraries, antibody libraries produced using such methods, and variant antibodies. Presently, methods of improving antibody binding (affinity maturation assays) require the screening of vast libraries of antibody variants (often >1010) to identify a small fraction of variants with improved characteristics. The present invention involves taking the nucleotide sequence of the framework and complementarity determining region of a target antibody and identifying motifs which would be recognised by deamination somatic hypermutation enzymes. A small library of variants is then created which incorporate one or more of these mutations. It was found that a relatively high proportion of the variants have an increased affinity. The technique of the present invention was demonstrated on the trastuzumab and Cathepsin S antibodies, and the variants produced are also claimed.

Abstract: The invention relates to HER3/HER2 bispecific antibodies binding to the beta-hairpin of HER3 and domain II of HER2, their preparation and use as medicament.

Abstract: The invention relates to specific anti-HER3 antibodies, that bind to the beta-hairpin of HER3, their preparation and use as medicament.

Abstract: The invention relates to HER3/HER2 bispecific antibodies binding to the beta-hairpin of HER3 and domain II of HER2, their preparation and use as medicament.

Abstract: The invention relates to specific anti-HER3 antibodies, that bind to the beta-hairpin of HER3, their preparation and use as medicament.

Abstract: Described are cross-specific antibody molecules with binding specificity for both AREG and HBEGF. The antibody molecules may be used in methods of treatment of cancer and diseases associated with angiogenesis.

Abstract: Described are cross-specific antibody molecules with binding specificity for both AREG and HBEGF. The antibody molecules may be used in methods of treatment of cancer and diseases associated with angiogenesis.

Abstract: A method of inhibiting activity of a cathepsin L-like protease in cells or tissue and the use of the method in the treatment of disease such as cancer and inflammatory diseases is described. The method comprises administration of a cathepsin propeptide or a nucleic acid encoding a cathepsin propeptide. In particular embodiments, the propeptide is a Cathepsin S propeptide. Further, the use of propeptides having an Fc portion is described.

Abstract: Described is a method of producing a soluble bioactive domain of a protein, the method comprising the step of selecting suitable soluble subunits of a protein and assessing the produced protein for desired activity. The method may comprise the steps of amplifying DNA encoding at least one candidate soluble domain, cloning the amplified DNA into at least one expression vector, using each of said vectors into which the DNA has been cloned to each transfect or transform one or more host cell strains, expressing said DNA in one or more host cell strains, and analyzing expression products from said host cells for solubility.