Abstract: This invention relates to a novel form of protein C or activated protein C. More specifically, the invention is directed to a variant of protein C that is activated at a higher rate than wild-type or other variants and produces an activated protein C with reduced anticoagulant properties while retaining the protective anti-inflammatory and anti-apoptotic properties of wild-type activated protein C. This novel APC variant will be beneficial for treating inflammatory and apoptotic disorders with a reduced risk for bleeding.

Abstract: A Ca2+ dependent recombinant antibody that specifically binds to a specific twelve peptide sequence (E D Q V D P R L I D G K) in the activation region of the Protein C has been constructed. The antibody does not bind to Activated Protein C and can be used to inhibit activation of Protein C by thrombin-thrombomodulin, in purification of Protein C, and in treatment of tumors.

Abstract: Mutant antithrombin modified to carry a more positive charge in the H-helix is provided. The modified antithrombin modulates the activities of thrombin, and extends the bioavailability of factor VIII.

Abstract: Mutant antithrombin modified to carry a more positive charge in the H-helix is provided. The modified antithrombin modulates the activities of thrombin, and extends the bioavailability of factor VIII.

Abstract: A method is disclosed to make any protein in a form that can be isolated rapidly from a solution using a specific monoclonal antibody designated "HPC-4". It has now been determined that it is possible to form a fusion protein of the epitope with a protein to be isolated, and isolate the protein using HPC-4-based affinity chromatography. In the preferred embodiment, a specific protease cleavage site is inserted between the epitope and the protein so that the epitope can be easily removed from the isolated protein. In an example, a functionally active soluble tissue factor including the twelve amino acid epitope recognized in combination with calcium by HPC-4 and a factor Xa cleavage site was expressed from a vector inserted into a procaryotic expression system. The recombinant tissue factor can be rapidly isolated in a single chromatographic step using the HPC-4 monoclonal antibody immobilized on a suitable substrate.