Ac-TVASSSTA is an Octapeptide mimic of the N-terminal residues of the reactive center loop of PAI-1. The Octapeptide inactivates PAI-1 by substituting for strand 4 in beta-sheet A in a manner that competes with formation of the latent species. Insertion of the peptide into beta-sheet A effectively forms a stable complex that converts PAI-1 into a substrate for tissue-type plasminogen activator (tPA) and other target proteinases. The resulting species of PAI-1 is thermodynamically stable and is useful for investigating the role of reactive center loop insertion.
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Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
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
FunctionThis 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.
Tissue specificityFound in plasma and platelets and in endothelial, hepatoma and fibrosarcoma cells.
Involvement in diseaseDefects 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.
Sequence similaritiesBelongs to the serpin family.
Post-translational modificationsInactivated by proteolytic attack of the urokinase-type (u-PA) and the tissue-type (TPA), cleaving the 369-Arg- -Met-370 bond.