SERPINE1. also known as plasminogen activator inhibitor-1 (PAI-1), is a key regulator of fibrinolysis and extracellular matrix remodeling. It inhibits tissue-type and urokinase-type plasminogen activators (tPA/uPA), thereby modulating plasmin generation and proteolytic activity. Overexpression of SERPINE1 is linked to pathological conditions such as thrombosis, fibrosis, cancer progression, and metabolic disorders, making it a biomarker and therapeutic target.
SERPINE1 antibodies are essential tools for detecting and quantifying this protein in research and diagnostics. They are widely used in techniques like Western blotting, immunohistochemistry (IHC), and enzyme-linked immunosorbent assays (ELISA) to study SERPINE1 expression patterns in tissues, cell cultures, or biological fluids. These antibodies help elucidate its role in disease mechanisms, such as its pro-fibrotic effects in organ fibrosis or its anti-apoptotic function in tumor survival.
Commercial SERPINE1 antibodies are typically raised against specific epitopes of the human protein, with polyclonal and monoclonal variants available. Validation steps, including knockout controls and cross-reactivity assessments, are critical due to potential homology with other serpin family members. Challenges include ensuring specificity across species (human, mouse, rat) and applications, as post-translational modifications or conformational changes may affect antibody binding. Researchers must carefully select antibodies validated for their intended experimental context to ensure reproducibility and accuracy.