Recombinant Human Serpin E1 (PAI-1) (carrier-free)
Description
PAI-1 was initially purified from bovine aortic endothelial cell culture. It is a member of the serine proteinase inhibitors (serpin) superfamily, which is divided into two groups: the inhibitory and non inhibitory serpins. PAI-1 is a globular protein that contains 3 beta-sheets and 9 alpha-helices. It possesses an exposed peptide loop and a reactive center loop (RCL), which is critical for the inhibitory mechanism. PAI-1 is the most important physiological inhibitor of tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA). Therefore, PAI-1 is the primary inhibitor of the process that produces the broad-spectrum serine protease plasmin from the zymogen plasminogen, and thus is the key regulator of the fibrinolytic system. PAI-1 forms a covalent bond with both t-PA and u-PA (1:1 molar ratio). It is known that several receptors (uPAR, LRP-1A, megalin, VLDLR, and LRP-1B) bind and mediate endocytosis of plasminogen activator - PAI-1 complexes. PAI-1 is present in blood and the extracellular matrix in a complex with vitronectin. Elevated PAI-1 levels have been implicated in the pathogenesis of atherosclerosis and myocardial infarction (MI). High levels of plasma PAI-1 in patients precede MI. Abnormal levels of PAI-1 are associated to metabolic syndrome, obesity, MI, obstructive nephropathy, cancer, cardiac fibrosis, pulmonary fibrosis, and bleeding thrombosis.