PAI-1 / SerpinE1 Protein (His Tag)

Plasminogen Activator Inhibitor 1 Protein

PAI-1 / SerpinE1 Protein Product Information

• Synonym: SERPINE1, PAI, PAI-1, PAI1, PLANH1
• Protein Construction: A DNA sequence encoding the human SerpinE1 precursor (NP_000593.1) (Met 1-Pro 402) was expressed with a C-terminal polyhistidine tag
• Source: Human
• Expression Host: Human Cells

PAI-1 / SerpinE1 Protein QC Testing

• Purity: > 97 % as determined by SDS-PAGE
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Val 24
• Molecular Mass: The mature recombinant human SerpinE1 consists of 390 amino acids and predicts a molecular mass of 44.2 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhSerpinE1 is approximately 45 kDa
• Formulation: Lyophilized from sterile 50mM NaAc, 0.1M NaCl, pH 5.5
• SDS-PAGE: PAI-1 / SerpinE1 protein

PAI-1 / SerpinE1 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

PAI-1 / SerpinE1 Protein Description

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors). Over 1000 serpins have been identified. Plasminogen activator inhibitor 1, also known as PAI-1, Endothelial plasminogen activator inhibitor, SERPINE1 and PLANH1, is a secreted protein which belongs to theserpin family. SERPINE1 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. Defects in PAI-1/SerpinE1 are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1 deficiency) which is characterized by abnormal bleeding due to PAI-1/SerpinE1 defect in the plasma. High concentrations of PAI-1/SerpinE1 have been associated with thrombophilia which is an autosomal dominant disorder in which affected individuals are prone to develop serious spontaneous thrombosis.

References

1. Sigurdardottir O., et al., 1994, Biochim. Biophys. Acta. 1208:104-10.
2. Liu, CX. et al.,2001, J. Biol. Chem. 276: 28889-96.
3. Forsyth, S. et al., 2003, Genomics 81: 336-45. 
4. Horvath, AJ. et al., 2004, J. Mol. Evol. 59: 488-97.
5. Steenbakkers PJ. et al., 2008, Mycol. Res. 112 (Pt 8): 999-1006.