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AB108894

Plasminogen activator Inhibitor Type 1 Human Chromogenic Activity Assay Kit

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(1 Publication)

Plasminogen activator Inhibitor Type 1 Human Chromogenic Activity Kit (ab108894) has been developed to determine human type I plasminogen activator inhibitor (PAI-1) activity in cell culture supernatant, serum, and plasma samples.

View Alternative Names

PAI1, PLANH1, SERPINE1, Plasminogen activator inhibitor 1, PAI, PAI-1, Endothelial plasminogen activator inhibitor, Serpin E1

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Functional Studies - Plasminogen activator Inhibitor Type 1 Human Chromogenic Activity Assay Kit (AB108894)
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Supplier Data

Functional Studies - Plasminogen activator Inhibitor Type 1 Human Chromogenic Activity Assay Kit (AB108894)

Example of Standard Curve.

Representative Standard Curve using ab108894.

Key facts

Detection method

Colorimetric

Sample types

Cell culture supernatant, Plasma, Serum

Results type

Quantitative

Sensitivity

= 0.56 AU/mL

Range

0.625 - 20 IU/mL

Assay Platform

Microplate reader

Reactivity data

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Product details

Plasminogen activator Inhibitor Type 1 Human Chromogenic Activity Kit (ab108894) has been developed to determine human type I plasminogen activator inhibitor (PAI-1) activity in cell culture supernatant, serum, and plasma samples.

A fixed amount of tissue-type plasminogen activator (tPA) is added in excess to undiluted sample, which allows PAI-1 and tPA to form an inactive complex. The assay measures plasminogen activation by residual tPA in coupled assays that contain tPA, plasminogen, and a plasmin-specific synthetic substrate. The amount of plasmin produced is quantitated using a highly specific plasmin substrate releasing a yellow para-nitroaniline (pNA) chromophore. The absorbance of the pNA at 405 nm is inversely proportional to the PAI-1 enzymatic activity.

Upon arrival, immediately store components of the kit at recommended temperatures. Avoid repeated freeze-thaw cycles.

Type I plasminogen activator inhibitor (PAI-1) is a 50 kDa serpin family member that inhibits tissue- and urokinase-type plaminogen activators (t-PA, u-PA). This protein appears to be an important regulator of plasminogen activation by t-PA and extracellular proteolysis by u-PA. The plasminogen activator proteolytic enzyme systems are important not only for fibrinolysis but also for extracellular matrix remodeling, and have been implicated in a number of normal and pathological processes including angiogensis, ovulation and embryogenesis, thrombotic and hemorrhagic disorders, connective tissue diseases, neoplasm and sepsis. PAI-1 is a prognosticator in breast cancer, gastric cancer, various forms of lung cancer and cervical cancer.

What's included?

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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
Multi
Storage information
Please refer to protocols

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Plasminogen Activator Inhibitor 1 (PAI-1) also known as SERPINE1 mechanically acts as an important regulator of fibrinolysis. It does this by inhibiting tissue plasminogen activator (tPA) and urokinase (uPA) which convert plasminogen to plasmin an enzyme that digests fibrin clots. PAI-1 is a single-chain glycoprotein with a molecular mass of approximately 50 kDa. It expresses in many tissues including liver adipose tissue and endothelial cells and has an important role in maintaining the balance between clot formation and dissolution.
Biological function summary

PAI-1 has essential functions in processes beyond fibrinolysis. It participates in extracellular matrix remodeling cell migration and tissue repair. PAI-1 interacts with vitronectin in plasma forming a complex that stabilizes its inhibitory function. This interaction affects angiogenesis and wound healing by modulating cell adhesion and migration highlighting PAI-1's versatility in different biological processes.

Pathways

PAI-1 significantly influences hemostasis and cell signaling networks. It plays a role in the plasminogen activation system a vital aspect of the hemostatic pathway which prevents excessive blood clot formation. Furthermore PAI-1 interacts with transforming growth factor-beta (TGF-β) in signaling pathways involved in cellular regulation. These interactions highlight PAI-1's link to proteins such as tPA and uPA which are critical in modulating fibrinolytic activity.

Elevated levels of PAI-1 are often associated with conditions like thrombosis and atherosclerosis. Thrombosis results from excessive fibrin formation due to insufficient plasminogen activation implicating PAI-1's inhibition in tPA and uPA activity. In cardiovascular disease contexts such as atherosclerosis PAI-1 influences the stability of atherosclerotic plaques. It also associates with diseases featuring excessive fibrosis due to PAI-1's regulatory effect on TGF-β-mediated pathways highlighting its connection to the pathological processes in both thrombosis and cardiovascular disorders.

Product protocols

Target data

Serine protease inhibitor. Inhibits TMPRSS7 (PubMed : 15853774). Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots (PubMed : 17912461, PubMed : 8481516, PubMed : 9207454, PubMed : 21925150). As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading (PubMed : 9175705). Acts as a regulator of cell migration, independently of its role as protease inhibitor (PubMed : 15001579, PubMed : 9168821). It is required for stimulation of keratinocyte migration during cutaneous injury repair (PubMed : 18386027). It is involved in cellular and replicative senescence (PubMed : 16862142). Plays a role in alveolar type 2 cells senescence in the lung (By similarity). Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis (PubMed : 25808697, PubMed : 27046084).
See full target information SERPINE1

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Molecular neurobiology 60:6441-6465 PubMed37458985

2023

Extracellular Vesicle-Serpine-1 Affects Neural Progenitor Cell Mitochondrial Networks and Synaptic Density: Modulation by Amyloid Beta and HIV-1.

Applications

Unspecified application

Species

Unspecified reactive species

Ibolya E András,Nelson Serrano,Irina Djuraskovic,Nikolai Fattakhov,Enze Sun,Michal Toborek
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