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Cardiovascular Blood Fibrinolysis / Thrombolysis

Recombinant Human PAI1 protein (ab185862)

Key features and details

  • Expression system: Mammalian
  • Purity: > 95% SDS-PAGE
  • Endotoxin level:
  • Tags: His tag C-Terminus
  • Suitable for: SDS-PAGE, HPLC

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Preparation and Storage

  • Alternative names

    • Clade E
    • Endothelial plasminogen activator inhibitor
    • Nexin
    • Nexin plasminogen activator inhibitor type 1
    • 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
    • Serine proteinase inhibitor clade E member 1
    • serpin
    • 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
  • 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
    modifications

    Inactivated by proteolytic attack of the urokinase-type (u-PA) and the tissue-type (TPA), cleaving the 369-Arg-
    -Met-370 bond.
  • Cellular localization

    Secreted.
  • Target information above from: UniProt accession P05121 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

Images

Please note: All products are "FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC PROCEDURES"
For licensing inquiries, please contact partnerships@abcam.com

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