Plasminogen Activator Inhibitor-1 (PAI-1, Serpin E1) is a member of the serpin family of serine protease inhibitors, and is the primary inhibitor of urokinase and tissue plasminogen activator (tPA). PAI-1 is expressed predominantly in adipose, liver and vascular tissues, but is also produced by certain tumor cells. Elevated levels of PAI-1 are associated with obesity, diabetes and cardiovascular disease, and increased production of PAI-1 is induced by various obesity-related factors, such as TNFα, glucose, insulin, and very-low-density lipoprotein. The obesity-related elevation of PAI-1 levels, along with the consequential deficiency in plasminogen activators, can lead directly to increased risk of thrombosis and other coronary diseases. Accordingly, PAI-1 has been implicated as an important molecular link between obesity and coronary disease. PAI-1 can also specifically bind vitronectin (VTN) to form a stable active complex with an increased circulatory half-life relative to free PAI-1. Recombinant Human PAI-1 is a 42.7 kDa protein containing 379 amino acid residues.
Amino Acid Sequence
Determined by its inhibitory effect against single chain tPA induced cleavage of a chromogenic substrate in Imidazole Buffer at 37°C. Half maximal inhibition against 1.0 µg/ml of single chain tPA was obtained at a concentration of 2.0 µg/ml.
Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1–1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at –20°C to –80°C.