| tPA Products |
| Tissue-type Plasminogen Activator (tPA) Proteins, Antibodies and Assays |
 tPA is a fibrin specific activator of plasminogen that is produced in endothelial cells with a normal concentration of 5-10 ng/mL in plasma. The fibrin specificity is the result of the interaction of the kringle-2 domain of tPA with specific lysine residues on fibrin.
Nascent tPA is comprised of a single polypeptide chain. Its proteolytic cleavage at a centrally located arginine-isolucine bond by plasmin gives rise to a 2-chain form, composed of the N-terminal derived heavy chain and the C-terminal light chain that are linked by a disulfide bond. The majority of tPA in circulation is present as a complex with PAI-1. PAI-1 acts as an inhibitor to tPA by binding to tPA and thus stifling its ability to activate plasmin. tPA activity is an indicator of both myocardial infarction for patients with impaired fibrinolytic systems as well as a marker for type-II diabetes.
Recombinant tPA is produced as an active single chain molecule with a molecular weight of approximately 70 kDa which can be cleaved by fibrin to the more active 2-chain form. |
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| uPA Products |
| Urokinase-type Plasminogen Activation (uPA) Proteins, Antibodies and Assays |
Urokinase-type Plasminogen Activator (uPA), also referred to as Urokinase, rapidly cleaves plasminogen, yielding plasmin. The key role of uPA in the firbrinolytic cascade is rapidly inhibited by the major modulator of fibrinolysis, PAI-1. uPA, when complexed with urokinase-type Plasminogen Activator Receptor (uPAR), functions to degrade the basement membrane and peritumoral matrix to facilitate the migration of tumor cells.
There are two forms of uPA, a 31 kDA low molecular weight (LMW) form and a 55 kDa high molecular weight (HMW) form. Autoproteolysis of HMW urokinase results in LMW urokinase and an 18.5 kDa amino terminal fragment (ATF). The ATF has been shown to inhibit proliferation and invasion of cancer cells by binding to the uPA receptor.
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