Human UPA ELISA Kit

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, along with its receptor uPAR, initiates a proteolytic cascade that results in the conversion of Plasminogen to Plasmin. Clinical studies have indicated that high uPA levels may elevate the risk for tumor invasion and metastasis Increased expression and activity can exert potent arthritogenic properties in rheumatoid arthritis patients. Increased uPA activity may be an implication for the pathophysiology of endometriosis.

Samples of Human plasma, serum, urine, cell culture media, or tissue extracts.