Recombinant Human PAI1 protein (Mutant) (ab233748)
Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Suitable for: SDS-PAGE
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Product name
Recombinant Human PAI1 protein (Mutant)
See all PAI1 proteins and peptides -
Purity
> 95 % SDS-PAGE.
A single substitution at position P14 (P14 arginine mutant) in the reactive center loop produces a PAI1 that becomes a substrate for proteinases rather than an inhibitor. Reactive center loop insertion follows protease cleavage and the PAI1 loses vitronectin binding properties. This molecule is useful for mechanistic studies. -
Expression system
Escherichia coli -
Accession
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Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Additional sequence information
P14 Arginine mutant.
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Preparation and Storage
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Alternative names
- Clade E
- Endothelial plasminogen activator inhibitor
- Nexin
see all -
Function
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. -
Tissue specificity
Found in plasma and platelets and in endothelial, hepatoma and fibrosarcoma cells. -
Involvement in disease
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. -
Sequence similarities
Belongs 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. -
Cellular localization
Secreted. - Information by UniProt
