Abstract: Hypercoagulable and hyperinflammatory responses can lead to a variety of diseases including but not limited to disseminated intravascular coagulation in sepsis, consumptive coagulopathy in trauma, thrombosis in the postsurgical setting, acute respiratory distress syndrome in lung, and other diseases or conditions. Polyphosphate is accumulated by many infectious microorganisms and may be released by damaged infectious microorganisms. In addition, polyphosphate is found in many organs and is released from activated platelets and mast cells. Polyphosphates activate the intrinsic pathway of coagulation that also induces inflammation. Hypercoagulable and hyperinflammatory challenge are mediators contributing to endothelial dysfunction, organ failure and death, which occur in many pathological conditions.

Abstract: An assay to assess thrombotic risk in which oxidized lipids comprising phospholipids are utilized as a membrane source in a clotting assay and the results compared to an assay in which unoxidized phospholipid is used as a membrane source in the presence and absence of activated protein C (“APC”). The assay can monitor for the presence of antibodies in the patient which interfere specifically with the anticoagulant function of APC in an oxidation dependent or independent manner. This can indicate the propensity of the patient to experience episodes of vein thrombosis or arterial thrombosis.

Abstract: Small, buffer soluble polypeptides having amino acid structures corresponding to residues 234-486, 310-486, and 407-486, of thrombomodulin and functionally equivalent analogs thereof inhibiting the clotting activity of thrombin and increasing protein C activation. The polypeptides can be coated onto the surface of articles adapted for contacting mammalian blood to render the surface non-thrombogenic. In pharmaceutical compositions, the polypeptides act as a natural anticoagulant.

Abstract: A Ca.sup.2+ dependent monoclonal 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. The antibody does not bind to Activated Protein C and can be used to inhibit activation of Protein C by thrombin-thrombomodulin. The antibody can be isolated from cell culture or ascites fluid in large quantities by affinity chromatography with mild conditions using the peptide bound to an immobilized substrate.The antibody has a number of specific uses in isolation and characterization of Protein C and as a model for the design of Ca.sup.2+ dependent antibodies for the isolation of other proteins, as a diagnostic, and as a therapeutic to prevent activation of Protein C. The Protein C can be naturally produced or produced by expression of the recombinant gene. Advantages of the antibody in purification of Protein C include the specificity for Protein C and not Activated Protein C, and the unique Ca.sup.

Abstract: A Ca.sup.2+ dependent monoclonal 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. The antibody does not bind to Activated Protein C and can be used to inhibit activation of Protein C by thrombin-thrombomodulin. The antibody can be isolated from cell culture or ascites fluid in large quantities by affinity chromatography with mild conditions using the peptide bound to an immobilized substrate. The antibody has a number of specific uses in isolation and characterization of Protein C and as a model for the design of Ca.sup.2+ dependent antibodies for the isolation of other proteins, as a diagnostic, and as a therapeutic to prevent activation of Protein C. The Protein C can be naturally produced or produced by expression of the recombinant gene. Advantages of the antibody in purification of Protein C include the specificity for Protein C and not Activated Protein C, and the unique Ca.sup.