| 説明 |
Plasminogen activator inhibitor-1 (serpin E1) is a serine protease inhibitor which belongs to the serpin family. Serpin E1 acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis. |
| Species |
Mouse
|
| Expression Host |
Human Cells
|
| Tag |
C-6His
|
| Accession Number |
G5E899
|
| 別名 |
Pai1, Planh1, Plasminogen activator inhibitor 1, Serpin E1, Mr1, Endothelial plasminogen activator inhibitor
|
| Amino Acid |
Phe22-Pro402
|
| Construction |
Recombinant Mouse Plasminogen Activator Inhibitor is produced by our Mammalian expression system and the target gene encoding Phe22-Pro402 is expressed with a 6His tag at the C-terminus.
|
| Protein Purity |
Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
|
| 分子量 |
50 KDa, reducing conditions
|
| Endotoxin |
Less than 1 EU/µg as determined by LAL test.
|
| Formulation |
Lyophilized from a 0.2 μm filtered solution of PBS, 5% Trehalose, 5% Mannitol, 0.02% Tween 80, 1mM EDTA, pH7.4.
|
| Reconstitution |
Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
|
| Stability & Storage |
Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.
Reconstituted protein solution can be stored at 2-8°C for 2-7 days.
Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
|
| Shipping |
The product is shipped at ambient temperature.
Upon receipt, store it immediately at the temperature listed below.
|
| Research Background |
Plasminogen activator inhibitor-1 (serpin E1) is a serine protease inhibitor which belongs to the serpin family. Serpin E1 acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.
|
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