Key features and details
- Expression system: Insect cells
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: Functional Studies, SDS-PAGE
Product nameRecombinant human PAI1 protein
See all PAI1 proteins and peptides
Biological activityKinetic Data: Second order rate constants for inhibition of: uPA = 6.3 X 106 M-1s-1 tPA = 5.7 X 106 M-1s-1 95 (+/-) 5% active by uPA titration
Purity> 95 % SDS-PAGE.
ab92772 is >98% pure by SDS-PAGE.
Expression systemInsect cells
Protein lengthFull length protein
Our Abpromise guarantee covers the use of ab92772 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Additional notesSolubility: > 2 mg/mL and < 5 mg/mL
The stable mutant contains mutations to confer additional stability to the otherwise labile molecule.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 0.82% Sodium phosphate, 0.0292% EDTA, 0.58% Sodium chloride
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- 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.
ab92772 has not yet been referenced specifically in any publications.