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- Tel: 858.663.9055
- Email: info@nsjbio.com
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PAI-1 antibody, also known as Plasminogen activator inhibitor 1 antibody, recognizes a secreted serine protease inhibitor encoded by the SERPINE1 gene and commonly referred to as Serpin E1 and endothelial plasminogen activator inhibitor. Plasminogen activator inhibitor 1 is a member of the serpin superfamily and is localized predominantly to the extracellular space and circulating plasma, where it tightly regulates fibrinolysis. It is highly expressed in endothelial cells, adipocytes, hepatocytes, platelets, smooth muscle cells, and various tumor cell types, with expression levels increasing in response to inflammatory cytokines, hypoxia, metabolic stress, and tissue injury.
Plasminogen activator inhibitor 1 functions as the primary physiological inhibitor of tissue-type plasminogen activator and urokinase-type plasminogen activator, thereby limiting plasmin generation and stabilizing fibrin clots. Through this antifibrinolytic activity, it plays a critical role in thrombosis, wound healing, and extracellular matrix remodeling. Beyond hemostasis, PAI-1 is actively involved in angiogenesis, cell adhesion, migration, and tumor invasion through interactions with vitronectin and the urokinase receptor complex. PAI-1 antibody is frequently used in studies investigating coagulation biology, vascular pathology, and tumor microenvironment signaling.
Structurally, Plasminogen activator inhibitor 1 contains the conserved reactive center loop characteristic of serpin family members, allowing it to form stable inhibitory complexes with target proteases. The protein exists in active, latent, and cleaved conformations, each with distinct functional implications. Binding to vitronectin stabilizes the active conformation and prolongs its half-life in circulation. Within tissues, PAI-1 is detected in the pericellular matrix and extracellular compartment, often co-localizing with integrins and components of the plasminogen activation system during dynamic remodeling processes.
Dysregulation of SERPINE1 expression is strongly associated with human disease. Elevated PAI-1 levels are linked to deep vein thrombosis, myocardial infarction, atherosclerosis, and other cardiovascular disorders characterized by impaired fibrinolysis. Increased expression is also observed in obesity and type 2 diabetes, contributing to metabolic and vascular complications. In oncology, high SERPINE1 expression correlates with poor prognosis in several malignancies, including breast, lung, and colorectal cancers, where it supports tumor cell survival, invasion, and resistance to apoptosis.
PAI-1 antibody supports research into TGF-beta signaling, hypoxia-inducible factor pathways, and inflammatory cytokine networks that regulate SERPINE1 transcription. Developmentally, PAI-1 expression increases during tissue repair and inflammatory responses, reflecting its role in controlled matrix turnover and immune regulation. Clone ABHG-19 recognizes Plasminogen activator inhibitor 1 and is suitable for detecting PAI-1 expression in relevant research applications.
Optimal dilution of the PAI-1/Plasminogen activator inhibitor 1 antibody should be determined by the researcher.
A synthetic peptide specific to human PAI1 / SERPINE1 was used as the immunogen for the PAI-1/Plasminogen activator inhibitor 1 antibody.
Store the PAI-1/Plasminogen activator inhibitor 1 antibody at -20oC.
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