Abstract: This invention concerns a family of chimeric antibodies with high affinities to a high molecular weight, tumor-associated sialylated glycoprotein antigen (TAG-72) of human origin. These antibodies have (1) high affinity animal VH and VL sequences which mediate TAG-72 binding and (2) human CH and CL regions. They are thought to produce significantly fewer side-effects when administered to human patients by virtue of their human CH and CL antibody domains. The nucleotide and amino acid sequences of VH&agr;TAG VH, CC46 VH, CC49H, CC83 VH, and CC92 VH, and CC49L, CC83 VL, and CC92 VL idiotype sequences are disclosed, as well as in vivo methods of treatment and diagnostic assay using these chimeric antibodies.

Abstract: This invention concerns a family of chimeric antibodies with high affinities to a high molecular weight, tumor-associated sialylated glycoprotein antigen (TAG-72) of human origin. These antibodies have (1) high affinity animal V.sub.H and V.sub.L sequences which mediate TAG-72 binding and (2) human C.sub.H and C.sub.L regions. They are thought to produce significantly fewer side-effects when administered to human patients by virtue of their human C.sub.H and C.sub.L antibody domains. The nucleotide and amino acid sequences of V.sub.H .alpha.TAG V.sub.H, CC46 V.sub.H, CC49.sub.H, CC83 V.sub.H, and CC92 V.sub.H, and CC49.sub.L, CC83 V.sub.L, and CC92 V.sub.L idiotype sequences are disclosed, as well as in vivo methods of treatment and diagnostic assay using these chimeric antibodies.

Abstract: This invention concerns a family of chimeric antibodies with high affinities to a high molecular weight, tumor-associated sialylated glycoprotein antigen (TAG-72) of human origin. These antibodies have (1) high affinity animal V.sub.H and V.sub.L sequences which mediate TAG-72 binding and (2) human C.sub.H and C.sub.L regions. They are thought to produce significantly fewer side-effects when administered to human patients by virtue of their human C.sub.H and C.sub.L antibody domains. The nucleotide and amino acid sequences of V.sub.H .alpha.TAG V.sub.H, CC46 V.sub.H, CC49.sub.H, CC83 V.sub.H, and CC92 V.sub.H, and CC49.sub.L, CC83 V.sub.L, and CC92 V.sub.L idiotype sequences are disclosed, as well as in vivo methods of treatment and diagnostic assay using these chimeric antibodies.

Abstract: The present invention discloses multivalent single chain antibodies which have two or more biologically active antigen binding sites. The multivalent single chain antibodies are formed by using a peptide linker to covalently link two or more single chain antibodies, each single chain antibody having a variable light domain linked to a variable heavy chain domain by a peptide linker.

Abstract: The present invention discloses multivalent single chain antibodies which have two or more biologically active antigen binding sites. The multivalent single chain antibodies are formed by using a peptide linker to covalently link two or more single chain antibodies, each single chain antibody having a variable light domain linked to a variable heavy chain domain by a peptide linker.

Abstract: The present invention discloses novel chimeric monoclonal antibodies directed against human carcinoembryonic antigen, having antigen-specific variable regions. DNA constructs for the light and heavy chain variable regions comprising the novel antibodies of the invention are also disclosed. Eukaryotic host cells capable of expression of the chimeric antibodies and comprising the novel chimeric antibody-encoding DNA constructs are also described.

Abstract: The present invention discloses novel chimeric monoclonal antibodies directed against human carcinoembryonic antigen, having antigen-specific variable regions. DNA constructs for the light and heavy chain variable regions comprising the novel antibodies of the invention are also disclosed. Eukaryotic host cells capable of expression of the chimeric antibodies and comprising the novel chimeric antibody-encoding DNA constructs are also described.