Celltech Therapeutics Limited

Celltech Limited

Celltech R&d Limited

Raymond John Owens

John Robert Adair

Mark William Bodmer

Geoffrey Thomas Yarranton

Martin John Perry

Andrew Mountain

Martyn Kim Robinson

David John King

Simon Mark Lumb

Alan Howard Lyons

Gregory Paul Winter

Terence Seward Baker

Lutz Riechmann

Nigel Richard Whittle

Humanized antibody molecules (HAMs) are described having specificity for human milk fat globule and having an antigen binding site wherein at least one of the complementarity determining regions (CDRs) of the variable domains is derived from the mouse monoclonal antibody CTMO1 and the remaining immunoglobulin-derived parts of the HAM are derived from a human immunoglobulin. The HAMs may be chimeric humanized antibodies or CDR-grafted humanized antibodies and are preferably produced by recombinant DNA techniques. The HAMs are useful for in vivo diagnosis and therapy.

Anti-HMFG antibodies and processes for their production

This invention relates to whole antibodies of neutral isotype having specificity for E-selection, process for their preparation (using vectors), pharmaceutical compositions containing them, and their use in therapy (e.g. for inflammatory disorders) and diagnosis. Said antibodies are variants of natural antibodies altered in the F region, especially in the CH domain, so that the interactions with antibodies F receptors and complement are absent or very low.

Antibodies against E-selectin

A33 antigen binding proteins are described for use in the diagnosis or treatment of colorectal tumors and metastases arising therefrom. The binding protein may be a humanized A33 antibody, including complete antibody molecules, fragments thereof, and particularly, multivalent monospecific proteins comprising two, three, four or more antibodies or fragments thereof, bound to each other by a cross-linking agent. For diagnosis or therapy, the humanized A33 antibody may be linked to a reporter or effector molecule.

Humanized antibodies directed against A33 antigen

Recombinant human phosphodiesterase type IVC is described, and DNA coding for it. Particular conformers of the enzyme are identified, including a R- and S-rolipram stereoselective conformer which is obtainable by expression of human phosphodiesterase type IVC DNA in mammalian or insect cells. The recombinant enzyme may be used in a screen to select a compound capable of modulating the action of the enzyme, or as an immunogen to generate an antibody.

Human phosphodiesterase type IVC, and its production and use

This invention relates to whole antibodies of neutral isotype having specificity for E-selectin, process for their preparation (using vectors), pharmaceutical compositions containing them, and their use in therapy and diagnosis. Said antibodies are variants of natural antibodies altered in the F,region, especially in the CH,domain, so that the interactions with antibodies F,receptors and complement are very low.

Methods for preparing Fv fragments which lack linking polypeptides in eukaryotic cells are provided.

Method for producing Fv fragments in eukaryotic cells

The present invention provides humanized antibody molecules (HAMs) having specificity for carcinoembryonic antigen (CEA) and having an antigen binding site wherein at least one of the complementarity determining regions (CDRs) of the variable domains is derived from the mouse monoclonal antibody A5B7 (A5B7 MAB) and the remaining immunoglobulin-derived parts of the HAM are derived from a human immunoglobulin. The HAMs may be chimeric humanized antibodies or CDR-grafted humanized antibodies and are preferably produced by recombinant DNA techniques. The HAMs are useful for in vivo diagnosis and therapy.

CDR grafted anti-CEA antibodies and their production

A multivalent antigen-binding protein comprises a first Fv fragment bound to at least one further Fv fragment by a connecting structure which links the Fv fragments to each other but which maintains them spaced apart such that the proteins are capable of binding to adjacent antigenic determinants. Typically the connecting structure comprises a spacing polypeptide sequence, which may be about 3 to 16 amino acids in length, connected to a linkage unit which may be a synthetic chemical linker, e.g., a maleimide linker, or is a polypeptide sequence leading from the spacing sequence. In a particularly preferred embodiment, the multivalent antigen binding protein comprises a VH domain having attached to its C-terminal end a V-C joining sequence and an antibody hinge sequence. Preferably one or more of the Fv fragments is a single chain Fv (scFv). The proteins are preferably prepared by recombinant DNA techniques and are useful for in vivo therapeutic and especially diagnostic applications.

Growing community of inventors

Henley-on-Thames, United Kingdom

Raymond John Owens