• NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • SpeciesHuman


Our Abpromise guarantee covers the use of ab92873 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Functional Studies


  • Purity> 95 % SDS-PAGE.

  • FormLiquid
  • Additional notesSolubility: > 2 mg/mL and < 5 mg/mL Spectrophotometric Data: Epsilon0.1% = 1.0

    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.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: 0.1M Sodium chloride, 0.05M Sodium phosphate, 1mM EDTA, pH 6.6

General Info

  • Alternative names
    • Clade E
    • Endothelial plasminogen activator inhibitor
    • Nexin
    • PAI
    • PAI 1
    • PAI-1
    • PAI1_HUMAN
    • PLANH1
    • 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 E1
    • Serpin peptidase inhibitor clade E
    • Serpin peptidase inhibitor clade E (nexin plasminogen activator inhibitor type 1) member 1
    • Serpine 1
    • SERPINE1
    see all
  • 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
    Inactivated by proteolytic attack of the urokinase-type (u-PA) and the tissue-type (TPA), cleaving the 369-Arg-
    -Met-370 bond.
  • Cellular localizationSecreted.
  • Information by UniProt

Recombinant Human PAI1 protein images

  • 10% SDS-PAGE
    Lane 1: ab92873 (3 ug) Reduced
    Lane 2: ab92873 (3 ug) + uPA (12 ug) Reduced
    Lane 3: Prestained Standard

References for Recombinant Human PAI1 protein (ab92873)

ab92873 has not yet been referenced specifically in any publications.

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