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PLAT, also known as plasminogen activator and tissue plasminogen activator, is a member of the peptidase S1 family. It is a heterodimer of chain A and chain B held by a disulfide bond. PLAT contains 1 EGF-like domain, 1 fibronectin type-I domain and 2 kringle domains. It is synthesized in numerous tissues (including tumors) and secreted into most extracellular body fluids, such as plasma, uterine fluid, saliva, gingival crevicular fluid, tears, seminal fluid, and milk. PLAT forms heterodimer with SERPINA5. It binds to fibrin with high affinity. It also binds to annexin A2, cytokeratin-8, fibronectin and laminin. Increased activity of plasminogen activator results in increased fibrinolysis of fibrin blood clots that is associated with excessive bleeding. Defective release of plasminogen activator results in hypofibrinolysis that can lead to thrombosis or embolism.