P05121

PAI-1 also known as SERPINE1 is a member of the serine proteinase inhibitor (serpin) superfamily. PAI-1 plays a crucial role in regulating fibrinolysis and tissue remodeling by inhibiting urokinase-type plasminogen activator (uPA) and tissue plasminogen activator (tPA), which are essential for the conversion of plasminogen to plasmin. This regulation is vital for maintaining hemostasis and preventing excessive tissue degradation, making PAI-1 a significant factor in various physiological and pathological processes, including wound healing, cancer progression, and cardiovascular diseases. PAI-1 can exist in both active and latent forms, with the latent form being able to regain activity through denaturation and renaturation, highlighting PAI-1′s dynamic role in the regulation of proteolytic activity. The ability of PAI-1 to fold into an inactive state without cleavage underscores the complexity of PAI-1′s function and importance in cellular processes.