Plasminogen (Y233) polyclonal antibody

Cleavage of the serine proteinase plasminogen to form plasmin is the central event in the dissolution of blood clots by the fibrinolytic system. Within the fibrinolytic cascade, the serine proteinases urokinase-type plasminogen activator (uPA) and tissue-type plasminogen activator (tPA) activate the proenzyme plasminogen by cleaving plasminogen to form the fibrinolytically active enzyme plasmin. The enzyme plasmin consists of a heavy chain of 561 amino acids, which originates from the N-terminus of plasminogen, and a light chain of 230 amino acid residues, which is derived from the C-terminus of plasminogen. Plasmin is a proangiogenic proteinase that is capable of degrading a variety of extracellular matrix proteins and that facilitates endothelial cell migration and angiogenesis. In the presence of free sulfhydryl donors (FSD), plasmin undergoes auto-proteolysis and is converted to the enzyme angiostatin, which blocks angiogenesis and neovascularization and can inhibit the growth of primary and metastatic tumors.