The present invention relates to a novel method for improving the viral safety of liquid Factor VII compositions, in particular those comprising active Factor VII polypeptides (a Factor VIIa polypeptide).

The present invention relates to novel human coagulation Factor VIIa variants having coagulant activity as well as polynucleotide constructs encoding such variants, vectors and host cells comprising and expressing the polynucleotide, pharmaceutical compositions, uses and methods of treatment.

The invention features a method of identifying therapeutically relevant compositions which include a therapeutic agent and 2,2-dimethylaminomethyl-[1-3]-dioxolane by screening for an effect of the agent on the liver of a model subject.

Provided herein are modified FVII polypetides, and modified FVIIa polypeptides, and methods of treatment of acute and episodic bleeding with modified FactorVIIa polypeptides. To effect treatment and use, in some embodiments, the modified polypeptides are subcutaneously administered to provide on-demand treatment. In some embodiments, the on-demand treatment is provided in a multiple dosing regimen over a twenty-four hour period. The subcutaneous administration of the modified polypeptides of the disclosure exhibit increased coagulant activity, potency, bioavailablilty and prolonged duration.

The present invention features inter alia nucleic acid molecules which encode polypeptides comprising a single chain Fc region and the polypeptides they encode. The Fc moieties of these constructs are linked by a cleavable scFc linker which is adjacent to at least one enzymatic cleavage site, e.g., an intracellular processing site. The resulting processed molecules comprise two polypeptide chains and substantially lack the extraneous amino acid sequence found in single chain Fc linker molecule. Methods of making and using these dimeric molecules are also described.

The invention concerns a combination comprising transgenic factor VII and a multispecific antibody directed against factor IX and X, for simultaneous or separate administration.

Materials and methods of in vivo possessing of target proteins in plants by co-expressing with proprotein processing enzyme, human Furin, are provided. A method of expressing highly soluble and functional active human Furin in plants also is provided.

Antibodies and antibody fragments that specifically bind to glycoprotein IIb/IIIa (GPIIb/IIIa) are disclosed. Chimeric molecules comprising such antibodies or antigen-binding fragments are also disclosed. In addition, methods of using the disclosed antibodies, antibody fragments, and chimeric molecules, e.g., to target agents to platelets and for the treatment or prevention of diseases or disorders are provided.

Provided herein are methods and immunoconjugate dimer compositions for the treatment of diseases associated with angiogenesis and neovascularization. In one aspect, the invention relates to a method for treating wet age-related macular degeneration (AMD) in an eye of a patient in need thereof. The method comprises administering to the patient in multiple dosing sessions, a composition comprising an effective amount of an immunoconjugate dimer, wherein the monomer subunits of the dimer each comprises a mutated human factor VIIa (fVIIa) protein conjugated to the human immunoglobulin G1 (IgG1) Fc domain.

The invention relates to materials and methods of conjugating a water soluble polymer to an oxidized carbohydrate moiety of a blood coagulation protein comprising contacting the oxidized carbohydrate moiety with an activated water soluble polymer under conditions that allow conjugation. More specifically, the present invention relates to the aforementioned materials and methods wherein the water soluble polymer contains an active aminooxy group and wherein an oxime linkage is formed between the oxidized carbohydrate moiety and the active aminooxy group on the water soluble polymer. In one embodiment of the invention the conjugation is carried out in the presence of the nucleophilic catalyst aniline. In addition the generated oxime linkage can be stabilized by reduction with NaCNBH.sub.3 to form an alkoxyamine linkage.