Recombinant Human 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).

Histidine Tag

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Ser22 & Val24

Lyophilized

The predicted molecular weight of Recombinant Human PAI-1, Serpin E1 is Mr 44 kDa. However, the actual molecular weight as observed by migration on SDS-PAGE is Mr 43 kDa.

44

This recombinant protein was 0.2 µm filtered and lyophilized from a sterile solution containing 10 mM sodium acetate (NaOAc) and Sodium chloride (NaCl), pH 6.0.

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.

Next Day Ambient

1. Ginsburg, D. et al. (1996) Blood. 87:4718
2. Declerck, PJ. et al. (1996) Biochem. 35:7474
3. Gelehrter, TD. 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, TM. et al. (1994) Blood Coagul. Fibrinol. 5:73