|Other Names||Plasminogen activator inhibitor 1, PAI, PAI-1, Endothelial plasminogen activator inhibitor, Serpin E1, SERPINE1, PAI1, PLANH1|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Serine protease inhibitor. Inhibits TMPRSS7 (PubMed:15853774). Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots (PubMed:8481516, PubMed:9207454, PubMed:17912461). As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading (PubMed:9175705). Acts as a regulator of cell migration, independently of its role as protease inhibitor (PubMed:15001579, PubMed:9168821). It is required for stimulation of keratinocyte migration during cutaneous injury repair (PubMed:18386027). It is involved in cellular and replicative senescence (PubMed:16862142). Plays a role in alveolar type 2 cells senescence in the lung (By similarity). Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis (PubMed:25808697, PubMed:27046084).|
|Tissue Location||Expressed in endothelial cells (PubMed:2430793, PubMed:3097076). Found in plasma, platelets, and hepatoma and fibrosarcoma cells.|
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This gene encodes a member of the serine proteinaseinhibitor (serpin) superfamily. This member is the principalinhibitor of tissue plasminogen activator (tPA) and urokinase(uPA), and hence is an inhibitor of fibrinolysis. Defects in thisgene are the cause of plasminogen activator inhibitor-1 deficiency(PAI-1 deficiency), and high concentrations of the gene product areassociated with thrombophilia. Alternatively spliced transcriptvariants encoding different isoforms have been found for this gene.
Ma, Z., et al. Biochem. Biophys. Res. Commun. 400(4):569-574(2010)Ince, D.A., et al. Genet Test Mol Biomarkers 14(5):643-647(2010)Bern, M.M., et al. Clin. Appl. Thromb. Hemost. 16(5):574-578(2010)Markl, B., et al. J Surg Oncol 102(3):235-241(2010)de Haas, E.C., et al. Cancer (2010) In press :
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