PAI-1
PAI-1 (plasminogen activator inhibitor 1, encoded by SERPINE1) is a secreted serine protease inhibitor of the serpin family. It is the principal inhibitor of tissue-type and urokinase-type plasminogen activators, and it is also known as PAI, PAI1 and PLANH1. Browse Assay Genie's current range of PAI-1 research reagents below, or read on for the biology behind the target.
PAI-1 is a serine protease inhibitor and a primary inhibitor of tissue-type plasminogen activator (PLAT, tPA) and urokinase-type plasminogen activator (PLAU, uPA). By inhibiting PLAT, it is required for down-regulation of fibrinolysis and for the controlled degradation of blood clots. By inhibiting PLAU, it contributes to the regulation of cell adhesion and spreading. It also inhibits TMPRSS7. Independently of its activity as a protease inhibitor, PAI-1 acts as a regulator of cell migration, and it is required for stimulation of keratinocyte migration during cutaneous injury repair.
The PAI-1 protein is secreted and belongs to the serpin family. It is involved in cellular and replicative senescence and plays a role in the senescence of alveolar type 2 cells in the lung. It also takes part in the regulation of cementogenic differentiation of periodontal ligament stem cells, and it regulates odontoblast differentiation and dentin formation during odontogenesis. The PAI-1 gene product has additionally been described as a component of innate antiviral immunity.
The SERPINE1 gene belongs to the serpin peptidase inhibitor gene group. Its previous HGNC name was serine (or cysteine) proteinase inhibitor, clade E (nexin, plasminogen activator inhibitor type 1), member 1. Defects in the gene cause plasminogen activator inhibitor-1 deficiency (PAI-1 deficiency), while high concentrations of the gene product are associated with thrombophilia. Mouse and rat each have a Serpine1 ortholog, which is useful for comparative studies of fibrinolysis and tissue repair.
PAI-1 is the principal inhibitor of tPA and uPA, so it is central to studies of fibrinolysis down-regulation and blood clot degradation.
High concentrations of PAI-1 are associated with thrombophilia, while PAI-1 deficiency results from defects in SERPINE1.
PAI-1 regulates cell migration independently of protease inhibition and is required for keratinocyte migration during cutaneous injury repair.
PAI-1 is involved in cellular and replicative senescence, lung alveolar type 2 cell senescence, and odontogenic and cementogenic differentiation.
PAI-1 is a serine protease inhibitor that acts as a primary inhibitor of tPA and uPA. Through tPA inhibition it down-regulates fibrinolysis and controls blood clot degradation. It also regulates cell adhesion, spreading and migration, and contributes to senescence and tissue repair.
PAI-1 is encoded by SERPINE1 (serpin family E member 1). Aliases include PAI, PAI1 and PLANH1. The earlier HGNC name was serine (or cysteine) proteinase inhibitor, clade E (nexin, plasminogen activator inhibitor type 1), member 1.
Defects in SERPINE1 cause PAI-1 deficiency, and high PAI-1 concentrations are associated with thrombophilia. Mouse and rat both have a Serpine1 ortholog; check the datasheet of any product for its validated reactivity.
Other serpin family members with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P05121; product specifications from Assay Genie datasheets.