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Recombinant Human SerpinE1/PAI-1 Protein (His Tag)
SKU: PDMH100015-100
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Recombinant Human SerpinE1/PAI-1 Protein (His Tag)
| SKU # | PDMH100015 |
| Expression Host | HEK293 Cells |
Description
| Synonyms | Endothelial Plasminogen Activator Inhibitor, PAI, PAI-1, PAI1, PLANH1, Plasminogen Activator Inhibitor 1, SERPINE1, Serpin E1 |
| Species | Human |
| Expression Host | HEK293 Cells |
| Sequence | Val24-Pro402 |
| Accession | P05121 |
| Calculated Molecular Weight | 43.8 kDa |
| Observed Molecular Weight | 48 kDa |
| Tag | C-His |
| Bio-activity | Not validated for activity |
Properties
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation | Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4. Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis |
Background
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.