Human PAI1 UPA Complex ELISA Kit

Plasminogen Activator Inhibitor 1 (PAI1) is the principal inhibitor of Tissue Plasminogen Activator (tPA) and Urokinase (uPA), the activators of Plasminogen and hence fibrinolysis. It is a serine protease inhibitor (serpin) protein (SERPINE1). PAI1 is mainly produced by the endothelium, but is also secreted by other tissue types, such as adipose tissue. Urokinase Plasminogen Activator (uPA) is a serine protease involved in degradation of the extracellular matrix and possibly tumor cell migration and proliferation. A specific polymorphism in this gene may be associated with late-onset Alzheimer's disease and also with decreased affinity for fibrin-binding. This protein converts Plasminogen to Plasmin by specific cleavage of an Arg-Val bond in Plasminogen. Plasmin in turn cleaves this protein at a Lys-Ile bond to form a two-chain derivative in which a single disulfide bond connects the amino-terminal A-chain to the catalytically active, carboxy-terminal B-chain. This two-chain derivative is also called HMW-uPA (High Molecular Weight uPA). HMW-uPA can be further processed into LMW-uPA (Low Molecular Weight uPA) by cleavage of chain A into a short chain A (A1) and an ATF-uPA (Amino-Terminal Fragment uPA). LMW-uPA is proteolytically active but does not bind to the uPA Receptor (uPAR). Urokinase Plasminogen Activator (uPA/PLAU) is a serine protease that activates Plasminogen to Plasmin in the blood fibrinolytic system. It is also implicated in events related to cell invasion/migration. Plasminogen Activator Inhibitor type 1 (PAI1/SERPINE1) is involved in the regulation of the blood fibrinolytic system and forms a 1:1 covalent complex with uPA and Tissue Plasminogen Activator (tPA/PLAT).

Samples of Human plasma, serum, urine, cell culture media, or tissue extracts may be applied directly to the plate.