Recombinant Human LMW Urokinase *di

Store in working aliquots at -80C. Avoid repeated freeze-thaw cycles.

Urokinase Plasminogen Activator (uPA) is involved in degradation of the extracellular matrix and possibly tumor cell migration and proliferation. 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 amino-terminal fragment. LMW-uPA is proteolytically active but does not bind to the uPA receptor. Recombinant Human LMW-uPA is produced in insect cell culture as the single-chain LMW form for plasminogen activation and receptor binding studies. The low molecular weight form of uPA is purified by auto-catalytic digestion of recombinant human urokinase, contains the proteinase domain, and is separated from the amino terminal fragment by cleavage at the Lys135-Lys136 bond.

2.5 mg/ml