Abstract: Systems and methods for imaging and tracking fibrin formation via interaction of a test sample with a clotting agent or for imaging and tracking fibrin removal by an anti-clotting agent are described.

Abstract: The assay of soluble endothelial protein C receptor (sEPCR) is useful to monitor effective thrombin levels and a hypercoagulable state. An assay for sEPCR is therefore useful to monitor ongoing effectiveness of anticoagulant therapy. A sEPCR ELISA assay is particularly useful for this purpose. A state of hypercoagulability in patients or normal individuals can also be identified by such an assay.

Abstract: The assay of soluble endothelial protein C receptor (sEPCR) is useful to monitor effective thrombin levels and a hypercoagulable state. An assay for sEPCR is therefore useful to monitor ongoing effectiveness of anticoagulant therapy. A sEPCR ELISA assay is particularly useful for this purpose. A state of hypercoagulability in patients or normal individuals can also be identified by such an assay.

Abstract: The assay of soluble endothelial protein C receptor (sEPCR) is useful to predict cardiovascular disease, particularly atherosclerotic cardiovascular disease (ASCVD). An assay for sEPCR is therefore useful to identify individuals at risk of developing ASCVD. An sEPCR ELISA assay is particularly useful for this purpose. Elevated sEPCR is indicative of an increased risk of developing cardiovascular disease.

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: Plasma EPCR has been isolated, characterized and shown to block cellular protein C activation and APC anticoagulant activity. Plasma EPCR appears to be about 43,000 daltons and circulates at approximately 100 ng/ml (98.4.+-.27.8 ng/ml, n=22). Plasma EPCR bound activated protein C with an affinity similar to that of recombinant soluble EPCR (Kd.sub.app approximately 30 nM), and inhibits both protein C activation on an endothelial cell line and APC anticoagulant activity in a one-stage factor Xa clotting assay. Soluble plasma EPCR appears to attenuate the membrane-bound EPCR augmentation of protein C activation and the anticoagulant function of activated protein C. Soluble EPCR has also been detected in urine. Levels of soluble EPCR can rise in inflammatory disease associated with vascular injury and appear to be correlated with inflammation and disease states associated with abnormal coagulation.

Abstract: Plasma EPCR has been isolated, characterized and shown to block cellular protein C activation and APC anticoagulant activity. Plasma EPCR appears to be about 43,000 daltons and circulates at approximately 100 ng/ml (98.4.+-.27.8 ng/ml, n=22). Plasma EPCR bound activated protein C with an affinity similar to that of recombinant soluble EPCR (Kd.sub.app approximately 30 nM), and inhibits both protein C activation on an endothelial cell line and APC anticoagulant activity in a one-stage factor Xa clotting assay. Soluble plasma EPCR appears to attenuate the membrane-bound EPCR augmentation of protein C activation and the anticoagulant function of activated protein C. Soluble EPCR has also been detected in urine. Levels of soluble EPCR can rise in inflammatory disease associated with vascular injury and appear to be correlated with inflammation and disease states associated with abnormal coagulation.

Abstract: A thrombin-binding substance derived from human tissue and having the characteristics of (a) molecular weight: 88,000.+-.20,000 in reduced condition and 71,000.+-.20,000 in unreduced condition; (b) isoelectric point: .sub.p H 4.2.+-.0.5; (c) affinity: strong for thrombin; (d) activities: capable of promoting the thrombin-catalyzed activation of protein C and prolonging clotting time; and (e) stability: stable over a .sub.p H range of 2 to 10 and stable to denaturing agents (sodium dodecylsulfate and urea) and to a pepsin treatment, is effectively useful for thrombolysis and anticoagulation.