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The region for expressing recombinant Human SERPINE1 contains amino acids 24-401. The theoretical molecular weight of the SERPINE1 protein is 46.7 kDa. This SERPINE1 protein is produced using e.coli expression system. The SERPINE1 coding gene included the N-terminal 6xHis tag, which simplifies the detection and purification processes of the recombinant SERPINE1 protein in following stages of expression and purification.Plasminogen activator inhibitor 1 (SERPINE1) is a member of the serine protease inhibitor (serpin) family and plays a crucial role in the regulation of fibrinolysis. SERPINE1 inhibits tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA), thus controlling the conversion of plasminogen to plasmin, a key enzyme in the dissolution of blood clots. Beyond its role in fibrinolysis, SERPINE1 is involved in various physiological and pathological processes, including tissue remodeling, inflammation, and cell migration. Dysregulation of SERPINE1 is implicated in conditions such as thrombosis, cardiovascular diseases, and cancer. Research on SERPINE1 explores its potential as a therapeutic target in diseases associated with altered fibrinolytic activity.
The region for expressing recombinant Human SERPINE1 contains amino acids 24-401. The theoretical molecular weight of the SERPINE1 protein is 46.7 kDa. This SERPINE1 protein is produced using e.coli expression system. The SERPINE1 coding gene included the N-terminal 6xHis tag, which simplifies the detection and purification processes of the recombinant SERPINE1 protein in following stages of expression and purification.Plasminogen activator inhibitor 1 (SERPINE1) is a member of the serine protease inhibitor (serpin) family and plays a crucial role in the regulation of fibrinolysis. SERPINE1 inhibits tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA), thus controlling the conversion of plasminogen to plasmin, a key enzyme in the dissolution of blood clots. Beyond its role in fibrinolysis, SERPINE1 is involved in various physiological and pathological processes, including tissue remodeling, inflammation, and cell migration. Dysregulation of SERPINE1 is implicated in conditions such as thrombosis, cardiovascular diseases, and cancer. Research on SERPINE1 explores its potential as a therapeutic target in diseases associated with altered fibrinolytic activity.
| Cat.No | ACP02871 | Target Name | SERPINE1 |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 24-401aa | Mol Weight | 46.7kDa |
| Protein Length | Partial | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P05121 |
|---|
Uniprot Id
P05121
Target Species
Human
Target Name
SERPINE1
Target Full Name
Plasminogen activator inhibitor 1
Target Function
Serine protease inhibitor. Inhibits TMPRSS7. Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots. As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading. Acts as a regulator of cell migration, independently of its role as protease inhibitor. It is required for stimulation of keratinocyte migration during cutaneous injury repair. It is involved in cellular and replicative senescence. Plays a role in alveolar type 2 cells senescence in the lung. Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis.
Target Involvement
Plasminogen activator inhibitor-1 deficiency (PAI-1D)
Target Subcellular Location
Secreted.
Target Protein Families
Serpin family
Target Tissue Specificity
Expressed in endothelial cells. Found in plasma, platelets, and hepatoma and fibrosarcoma cells.
Target Research Area
Cardiovascular
Target Synonyms
Clade E; Endothelial plasminogen activator inhibitor; Nexin ; Nexin plasminogen activator inhibitor type 1; PAI 1; PAI; PAI-1; PAI1_HUMAN; PLANH1; Plasminogen activator inhibitor 1; Plasminogen activator inhibitor type 1; Serine (or cysteine) proteinase inhibitor ; Serine (or cysteine) proteinase inhibitor clade E (nexin plasminogen activator inhibitor type 1) member 1; Serine proteinase inhibitor clade E member 1; serpin; Serpin E1; Serpin peptidase inhibitor clade E (nexin plasminogen activator inhibitor type 1) member 1; Serpin peptidase inhibitor clade E; Serpine 1; SERPINE1
Target Background
This gene encodes a member of the serine proteinase inhibitor (serpin) superfamily. This member is the principal inhibitor of tissue plasminogen activator (tPA) and urokinase (uPA), and hence is an inhibitor of fibrinolysis. The protein also functions as a component of innate antiviral immunity. Defects in this gene are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1 deficiency), and high concentrations of the gene product are associated with thrombophilia.
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