84-9364-13　Recombinant Human SerpinE1/PAI-1 Protein （His Tag）（Active） 50ug　PKSH031702

特徴

• 背景：Plasminogen activator inhibitor 1, also known as PAI-1, Endothelial plasminogen activator inhibitor, SerpinE1 and PLANH1, is a secreted glycoprotein which belongs to the serpin family.
• SerpinE1 is the primary physiological inhibitor of the two plasminogen activators urokinase （uPA） and tissue plasminogen activator （tPA）.
• Its rapid interaction with TPA may function as a major control point in the regulation of fibrinolysis.
• Defects in SerpinE1 are the cause of plasminogen activator inhibitor-1 deficiency （PAI-1 deficiency） which is characterized by abnormal bleeding due to SerpinE1 defect in the plasma.
• High concentrations of SerpinE1 have been associated with thrombophilia which is an autosomal dominant disorder in which affected individuals are prone to develop serious spontaneous thrombosis.
• Studies of PAI-1 have contributed significantly to the elucidation of the protease inhibitory mechanism of serpins, which is based on a metastable native state becoming stabilised by insertion of the RCL into the central beta-sheet A and formation of covalent complexes with target proteases.
• Greater expression of PAI-1 has been associated with increased survival of cells and resistance to apoptosis.
• PAI-1 appears to influence apoptosis by decreasing cell adhesion （anoikis） as well as its effect on intracellular signaling.
• PAI-1, in its active state, also binds to the extracellular protein vitronectin.
• When in complex with its target proteases, it binds with high affinity to endocytosis receptors of the low density receptor family.
• The mechanisms of PAI-1 overexpression during obesity are complex, and it is conceivable that several inducers are involved at the same time at several sites of synthesis.
• PAI-1 is also implicated in adipose tissue development.
• It suggests that PAI-1 inhibitors serve in the control of atherothrombosis.