Description_x000D_ Biochem/physiol Actions_x000D_ The activated form of plasminogen, plasmin, was shown to promote the migration of melanoma and lung tumor cells plated on the extracellular matrix protein laminin by altering protein kinase C signaling._x000D_ Plasminogen is the inactive precursor of the protease plasmin. Plasminogen is activated by the action of either tissue plasminogen activator (tPA), which primarily activates the fibrinolytic (thrombolytic) activity of plasmin, or urokinase plasminogen activator (uPA), which is associated with extracellular matrix remodeling and cell migration. Plasmin cleaves fibrin/fibrinogen and blood coagulation factors V/Va and VIII/VIIIa. It activates matrix metalloproteinases by cleaving the inactive proenzymes. It is also involved in the activation of some growth factors, such as vascular endothelial growth factor (VEGF) and transforming growth factor β (TGF-β)._x000D_ Other Notes_x000D_ ε-Aminocaproic acid free_x000D_ Unit Definition_x000D_ One unit will produce a ΔA275 of 1.0 from α-casein in 20 min at pH 7.5 at 37 °C, when measuring perchloric acid soluble products in a volume of 5.0 mL. Activity determined after activation to plasmin with urokinase._x000D_ Physical form_x000D_ Lyophilized powder containing NaCl, EDTA, lysine, and Tris buffer salts_x000D_ Reconstitution_x000D_ Solutions should be stored in buffer containing 20 mM lysine at neutral pH. The protein should be as concentrated as possible. Frozen in aliquots at −20 °C, it should be stable for several weeks.