Fibrinolysis and thrombosis are two opposing molecular processes in blood that are essential for maintaining the balance of blood clotting, and clot resolution, within the circulatory system. Thrombosis involves the formation of blood clots to prevent excessive bleeding after injury, whilst fibrinolysis is responsible for dissolving these clots once they are no longer needed, preventing the potential obstruction of blood vessels. Thrombosis begins when there is injury to a blood vessel. This injury exposes the underlying subendothelial matrix, releasing tissue factor (TF). Tissue factor interacts with circulating factor VII to form the TF-VIIa complex, initiating the extrinsic pathway of the coagulation cascade. The TF-VIIa complex activates factor X, leading to the conversion of prothrombin (factor II) to thrombin (factor IIa). Thrombin plays a central role in thrombosis, converting fibrinogen (factor I) into fibrin. Fibrin subsequently forms a mesh that stabilizes the clot by entrapping platelets and red blood cells. Thrombin also activates platelets, leading to their aggregation and further stabilization of the clot. Activated platelets release substances like ADP and thromboxane A2, which then attract more platelets and further enhance aggregation. Fibrinogen is converted to fibrin by thrombin. Fibrin monomers then polymerize into long strings of fibrin monomers creating a meshwork that physically strengthens the clot. This fibrin network traps red blood cells and platelets, forming the solid structure of the clot. Once the injured blood vessel is repaired and the clot is no longer needed, fibrinolysis is initiated. Plasminogen, an inactive precursor present in the blood, is activated to plasmin, a protease that degrades fibrin. Plasminogen is converted to plasmin through the action of tissue plasminogen activator (tPA) and urokinase plasminogen activator (uPA), both of which are released by endothelial cells. tPA is particularly important in initiating fibrinolysis in response to clot formation. When tPA binds to fibrin, it undergoes a conformational change that enhances its activity. This localized binding ensures that plasminogen activation occurs specifically at the site of the clot. Plasmin degrades the fibrin meshwork into smaller fragments called fibrin degradation products (FDPs). The proteolytic action of plasmin on fibrin causes the gradual breakdown of the clot structure. As more fibrin is cleaved, the clot becomes progressively weaker and less stable. This proteolytic process thereby serves to dissolve the clot and restores blood flow in the affected vessel. The fibrinolytic system is tightly regulated to prevent excessive bleeding or unwanted clot dissolution. Plasmin activity is controlled by inhibitors, such as α2-antiplasmin and plasminogen activator inhibitor-1 (PAI-1), which maintain a balance between clot degradation and clot stability. A precise regulation of thrombosis and fibrinolysis is critical to maintaining vascular health and preventing the formation of harmful blood clots that can lead to conditions like deep vein thrombosis, stroke, and heart attacks. We provide a comprehensive product catalogue of research tools for investigating fibrinolysis and thrombosis, including D-Dimer antibodies, C1 Inactivator antibodies, uPA Receptor antibodies, Angiotensinogen ELISA Kits, and Thrombospondin 1 ELISA Kits. Explore our full fibrinolysis and thrombosis product range below and discover more, for less.