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Plasmin is a serine protease central to the breakdown of blood clots through fibrinolysis, where it degrades fibrin, the main structural component of clots1. Beyond its primary role in fibrinolysis, plasmin also participates in fibrinogenolysis, complement activation, tissue remodeling, and inflammation. It is synthesized in the liver as the inactive precursor plasminogen, which circulates in the blood and is activated at sites of clot formation by tissue plasminogen activator (tPA), urokinase, or therapeutically by streptokinase. Structurally, plasmin contains multiple domains, including kringle domains that facilitate binding to lysine residues on fibrin and cell surfaces, enhancing its targeting and activity.
Functionally, plasmin not only dissolves clots but also activates collagenases, complement components (such as C1 and C5), and cleaves extracellular matrix proteins, contributing to processes like embryonic development, wound healing, and tumor invasion. Deficiencies or dysregulation of plasmin activity can lead to thrombosis or rare disorders such as plasminogen deficiency, which impairs wound healing and tissue repair. Clinically, plasmin and its activators are used as thrombolytic agents to treat conditions like myocardial infarction, stroke, and pulmonary embolism, and ongoing research explores engineered plasmin variants for safer, more targeted therapies.
Common uses include IVD Assay standards, calibrators and controls, coagulation research, cardiovascular research, therapeutics development.
Not a hazardous substance or mixture.
12 - Non Combustible Liquids
