|Purity||>95% by SDS PAGE|
Urokinase-type plasminogen activator is a serine protease involved in degradation of the extracellular matrix and possibly tumor cell migration and proliferation. It converts plasminogen to plasmin by specific cleavage of an Arg-Val bond in plasminogen.
The PLAU precursor is cleaved at a Lys-Ile bond by plasmin 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 (HMW-uPA). The low molecular weight uPA (LMW-uPA) is generated 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.
Immunofluorescence, FACS, ELISA, Western blot, protein-protein interactions, Pull-down assay,
PBS solution 1 mg/ml, contains 10 mM glutation.
For research use only. Not for use in diagnostic procedures.