Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Suitable for: SDS-PAGE
Product nameRecombinant 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 systemEscherichia coli
Protein lengthFull length protein
Additional sequence informationP14 Arginine mutant.
Our Abpromise guarantee covers the use of ab233748 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.
Constituents: 0.82% Sodium phosphate, 0.58% Sodium chloride, 0.03% EDTA
- Clade E
- Endothelial plasminogen activator inhibitor
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.
modificationsInactivated by proteolytic attack of the urokinase-type (u-PA) and the tissue-type (TPA), cleaving the 369-Arg-
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab233748 has not yet been referenced specifically in any publications.