Fibrinolysis is regulated by the plasminogen activators, tissue plasminogen activator (tPA) and urokinase PA (uPA), and by the plasminogen activator-inhibitors (PAIs). Two PAIs include the serpin family members, PAI-1 and PAI-2. PAI-1 is a glycoprotein found in plasma, platelets, endothelial cells, hepatoma cells, and fibrosarcoma cells. Thrombin, endotoxin, and IL-1 induce PAI-1 synthesis in endothelial cells, which is where the major portion of plasma PAI-1 is produced. PAI-2 is a glycoprotein expressed in placenta and monocyte macrophages. The uPA/plasmin system may play a key role in cancer progression through degradation of the extracellular matrix during tumor cell migration. Paradoxically, high levels of PAI-1 are also predictive of poor prognosis of cancer patients. This finding may be a result of the role of plasmin proteolysis in the prevention of tumor vessel assembly. PAI-1 can promote tumor angiogenesis, and the mechanism may involve PAI-induced regulation of plasmin proteolysis during tumor angiogenesis. Thus, PAI-1 is a serpin protease inhibitor that is important for the regulation of plasmin proteolysis during fibrinolysis and extracellular matrix degradation.
Host Species: Mouse
Species Reactivity [for Features Main]: Human
Immunogen: Human PAI-1 aa. 207-329
Immunofluorescence, Western Blotting
|Human PAI-1 aa. 207-329|
|Store undiluted at -20°C.|
|Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.|
For Research Use Only.
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