Urokinase-type Plasminogen Activator (u-PA)
Urokinase-type plasminogen activator (uPA), is a serine protease. It was discovered in 1947. Urokinase was originally isolated from human urine, but is present in several physiological locations, such as blood stream and the extracellular matrix. The primary physiological substrate is plasminogen, which is an inactive form (zymogen) of the serine protease plasmin. Activation of plasmin triggers a proteolysis cascade that, depending on the physiological environment, participates in thrombolysis or extracellular matrix degradation. This links urokinase to vascular diseases and cancer. The most important inhibitors of urokinase are the serpins plasminogen activator inhibitor-1 (PAI-1) and plasminogen activator inhibitor-2 (PAI-2), which inhibit the protease activity irreversibly. In the extracellular matrix, urokinase is tethered to the cell membrane by its interaction to the urokinase receptor.
TECHNOZYM® u-PA ELISA Kit
A highly sensitive sandwich ELISA for the quantitative determination of u-PA in human plasma and tissue extracts. The u-PA ELISA Kit is based on a monoclonal antibody used as a catching antibody and a second monoclonal peroxidase-labeled detecting antibody. Double and single chain urokinase can be detected.
TECHNOZYM® u-PA Combi Actibind® ELISA Kit
An ELISA for the combined quantitative determination of concentration and activity of u-PA in human plasma. TECHNOZYM® u-PA Combi Actibind® ELISA Kit is based on a catching antibody which does not interfere with the functional activity of u-PA. Following the binding of u-PA in the sample by the antibody, functional activity of bound u-PA is determined using chromogenic plasmin substrate. After measuring the functional activity, this determination system is washed away and bound u-PA antigen is detected using a peroxidase-labeled monoclonal anti u-PA antibody which recognizes both free u-PA and u-PA inhibitor complexes.