Recombinant Human SerpinE1/PAI-1 Protein (His Tag)

Cat. No : CDRP-00570

size:

Target Information
Target Name	SerpinE1/PAI-1
Synonyms	Plasminogen Activator Inhibitor 1; PAI; PAI-1; Endothelial Plasminogen Activator Inhibitor; Serpin E1; SERPINE1; PAI1; PLANH1; SERPINE1
UniProt ID	P20333-2
Accession	P05121

Product Details
Expression Host	HEK293 Cells
Species	Human
Tag	C-His
Molar Mass	43.8 kDa
Sequence	Ala 31-Ala 678

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.

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.

Properties
Purity	>85% as determined by reducing SDS-PAGE.
Formulation	Lyophilized from a 0.2 μm filtered solution of 20 mM PBS, 150 mM NaCl, pH7.4.
Reconstitution	Please refer to the printed manual for detailed information.
Shipping	This product is provided as lyophilized powder which is shipped with ice packs.
Storage	Generally, 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.

! For research use only. Not intended for any clinical use.