Recombinant Human Plasminogen Activator Inhibitor-1 (PAI-1)

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) (1-2). It is also a major regulator of fibrinolysis and an important component of the acute phase response, the coordinated systemic reaction of an organism to tissue injury (3). PAI-1 is expressed predominantly in adipose, liver and vascular tissues and is also produced by certain tumor cells. It can also specifically bind vitronectin (VTN) to form a stable active complex with an increased circulatory half life relative to free PAI-1 (4). 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 (5). PAI1 deficiency may represent an inherited autosomal recessive bleeding disorder (6).

Lyophilized

The predicted molecular weight of Recombinant Human PAI-1 is Mr 43 kDa.

43

This recombinant protein was 0.2 µm filtered and lyophilized from modified Dulbecco’s phosphate buffered saline (1X PBS) pH 7.5 with no calcium, magnesium, or preservatives.

This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.

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1. Ginsburg, D. et al. (1996) Blood 87:4718 2. Declerck, P. J. et al. (1996) Biochem. 35:7474 3. Gelehrter, T. D. et al. (1996) J. Cell. Physiol. 168:648 4. Schroeck, F. et al. (2003) Biol. Chem. 383:1143 5. De Taeye, B. et al. (2005) Curr. Opin. Pharmacol. 5:149 6. Reilly, T. M. et al. (1994) Blood Coagul. Fibrinol. 5:73