The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
A single mutation results in nearly complete loss of binding of the PAI1 mutant to the important ligand vitronectin. All other aspects of PAI1 biological activity such as anti protease activity remain unaffected.
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Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Endothelial plasminogen activator inhibitor
Plasminogen activator inhibitor 1
Plasminogen activator inhibitor type 1
Serine (or cysteine) proteinase inhibitor
Serine (or cysteine) proteinase inhibitor clade E (nexin plasminogen activator inhibitor type 1) member 1
Serpin peptidase inhibitor clade E
Serpin peptidase inhibitor clade E (nexin plasminogen activator inhibitor type 1) member 1
This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, and protein C. Its rapid interaction with TPA may function as a major control point in the regulation of fibrinolysis.
Found in plasma and platelets and in endothelial, hepatoma and fibrosarcoma cells.
Defects in SERPINE1 are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1D) [MIM:613329]. It is a hematologic disorder characterized by increased bleeding after trauma, injury, or surgery. Affected females have menorrhagia. The bleeding defect is due to increased fibrinolysis of fibrin blood clots due to deficiency of plasminogen activator inhibitor-1, which inhibits tissue and urinary activators of plasminogen. Note=High concentrations of SERPINE1 seem to contribute to the development of venous but not arterial occlusions.
Belongs to the serpin family.
Inactivated by proteolytic attack of the urokinase-type (u-PA) and the tissue-type (TPA), cleaving the 369-Arg- -Met-370 bond.