Urokinase (uPA), a serine protease encoded by the PLAU gene, plays a key role in the plasminogen activation system, converting plasminogen to plasmin to degrade fibrin clots. Beyond fibrinolysis, uPA is involved in extracellular matrix remodeling, cell migration, and tissue repair. It is secreted as an inactive pro-enzyme (pro-uPA) and activated upon binding to its receptor (uPAR), forming a cell-surface signaling complex linked to pathological processes like cancer metastasis, chronic inflammation, and fibrosis.
Urokinase antibodies are immunological tools designed to target uPA or its components (e.g., pro-uPA, active uPA, uPAR). These antibodies are widely used in research to study uPA expression, localization, and function in diseases. For example, immunohistochemistry with anti-uPA antibodies helps visualize uPA distribution in tumor tissues, correlating its overexpression with poor prognosis in cancers. In therapeutic contexts, neutralizing anti-uPA/uPAR antibodies are explored to inhibit tumor invasion by blocking proteolytic activity or disrupting uPA-uPAR interactions. Some preclinical studies also investigate their potential in attenuating fibrosis or inflammatory disorders. Challenges include ensuring specificity due to structural similarities among serine proteases and optimizing delivery for clinical applications. Overall, urokinase antibodies serve as critical reagents for understanding uPA biology and developing targeted therapies.