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Human Plasminogen activator inhibitor-1, recombinant
Overview
The sequence corresponding to amino acids 24 to 402 of human PAI-1 (mature form) tagged with 6xHis on the carboxy-terminal was expressed in E. Coli.
Alternate Names
PAI 1
SERPINE1
PAI1
Background Information
Plasminogen activator inhibitor-1 (PAI-1) is a member of the serine protease inhibitor (serpin) superfamily and a central regulatory protein in the blood coagulation system. PAI-1 is unique among serpins in exhibiting distinct active and inactive (latent) conformations in vivo. Human PAI-1 is a single-chain glycoprotein with a molecular weight of 43 kDa. This inhibitor acts as "bait" for tissue-type and urokinase-type plasminogen activators (tPA and uPA) and protein C. Its rapid interaction with tPA may function as a major control point in the regulation of fibrinolysis. The highly mobile reactive-center loop (RCL) is thought to account for both the rapid inhibiton of plasminogen activators, and the rapid and spontaneous transition of the unstable, active form of PAI-1 into the stable, inactive conformation (t1/2 at 37oC, 2 hours). The inactive form can be partially reactivated by denaturants such as urea, guanidine hydrochloride or SDS. High concentrations of PAI-1 have been associated with human thromboembolic disease. PAI-1 activity may limit the extent of tumor metastasis, since uPA activity is a major contributory factor promoting dissolution of tumor matrix and basement membrane.
References
Product Information
Presentation
Liquid. In 150 mM Na2HPO4, pH 6.6, 500 mM NaCl, 2 mM Glutathione, and 0.01% Tween-80.
>/=98%, as determined by SDS-PAGE gel electrophores. Endotoxin level: < 1EU/microgram.
Specific Activity
By uPA activity assay, the recombinant PAI-1 contains a mixture of the active and latent forms, with > 45% of active form. To fully activate the latent PAI-1, the PAI-1 must be incubated in Activation Buffer (2X Activation Buffer: 8 M Guanidine HCl, 40 mM Sodium Acetate, pH 5.6, 400 mM NaCl, 0.2% Tween 20) for 15 to 30 minutes (Sancho, 1994). The recombinant PAI-1 is able to bind to uPA resulting in a SDS-stable complex.
Plasminogen activator inhibitor-1 (PAI-1) is the primary, fast-acting inhibitor of plasminogen activators. It is often bound to vitronectin, an abundant component of the extracellular matrix in many tissues. Protease nexin-1 is a potent serpin able to inhibit thrombin, plasmin, and plasminogen activators. PAI-1 and nexin-1 are members of the serpin superfamily and represent clade E. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones.
FUNCTION: This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, and protein C. Its rapid interaction with TPA may function as a major control point in the regulation of fibrinolysis. SUBUNIT STRUCTURE: Interacts with VTN. Binds LRP1B; binding is followed by internalization and degradation. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Found in plasma and platelets and in endothelial, hepatoma and fibrosarcoma cells. PTMs: Inactivated by proteolytic attack of the urokinase-type (u-PA) and the tissue-type (TPA), cleaving the 369-Arg-|-Met-370 bond. DISEASE: Defects in SERPINE1 are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1 deficiency) [MIM:173360]. This deficiency is characterized by abnormal bleeding due to SERPINE1 defect in the plasma. High concentrations of SERPINE1 have been associated with thrombophilia [MIM:188050]; an autosomal dominant disorder in which affected individuals are prone to develop serious spontaneous thrombosis.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Store at -80ºC. Thaw on ice and freeze aliquots at -80ºC for longer storage. This product is stable for at least 2 years as supplied. Avoid repeated freeze/thaw cycles.
Plasminogen activator inhibitor-1 (PAI-1) is a specific inhibitor of the serine proteases tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA). To systematically investigate the roles of the reactive center P1 and P1' residues in PAI-1 function, saturation mutagenesis was utilized to construct a library of PAI-1 variants. Examination of 177 unique recombinant proteins indicated that a basic residue was required at P1 for significant inhibitory activity toward uPA, whereas all substitutions except proline were tolerated at P1'. P1Lys variants exhibited lower inhibition rate constants and greater sensitivity to P1' substitutions than P1Arg variants. Alterations at either P1 or P1' generally had a larger effect on the inhibition of tPA. A number of variants that were relatively specific for either uPA or tPA were identified. P1Lys-P1'Ala reacted 40-fold more rapidly with uPA than tPA, whereas P1Lys-P1'Trp showed a 6.5-fold preference for tPA. P1-P1' variants containing additional mutations near the reactive center demonstrated only minor changes in activity, suggesting that specific amino acids in this region do not contribute significantly to PAI-1 function. These findings have important implications for the role of reactive center residues in determining serine protease inhibitor (serpin) function and target specificity.
