Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. They 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. Serpin E1 is a secreted protein which belongs to the Serpin family. Serpin E1 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 SERPINE1 are characterized by abnormal bleeding due to Serpin E1 defect in the plasma. High concentrations of Serpin E1 have been associated with thrombophilia which is an autosomal dominant disorder in which affected individuals are prone to develop serious spontaneous thrombosis.
Recombinant Human Serine Protease Inhibitor-clade E1 is produced by our Mammalian expression system and the target gene encoding Val24-Pro402 is expressed with a 6His tag at the C-terminus.
Purity:
> 95 % as determined by reducing SDS-PAGE.
Mol Mass:
43.8 kDa
AP Mol Mass:
48 kDa
Formulation:
Lyophilized from a 0.2 µm filtered solution of 20mM HAc-NaAc, 150mM NaCl, pH 4.0.
Shipping:
This product is provided as lyophilized powder which is shipped with ice packs.
Stability and Storage:
Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
system_update_altDatasheetHuman SerpinE1/PAI Recombinant Protein Plasminogen activator inhibitor 1, also known as PAI-1, Endothelial plasminogen activator inhibitor, SerpinE1 and PLANH1, is a sec
system_update_altDatasheetHuman SerpinB2/PAI-2 Recombinant Protein Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental bi
