Human PAI-1 (substrate form – P12 Arginine P14 Arginine double mutant)


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Human PAI-1 (substrate form – P12 Arginine P14 Arginine double mutant)

Two amino acid substitutions at positions P12 and P14 in the reactive center loop produces a PAI-1 that becomes a substrate for proteinases rather than an inhibitor. The reactive center loop does not insert following protease cleavage and the PAI-1 retains normal vitronectin binding. The double mutation also results in extended half-life compared to native PAI-1. This molecule is useful for mechanistic studies.
1. Huang, Y. et al. (2009) Am. J. Physiol. Renal Physiol. 297:F1045–F1054.
2. Courey, A.J. et al. (2011) Blood. 118:2313–2321.
3. Zhong, J. et al. (2014) Lab. Invest. 94:633–644.

Gene ID: 5054
Swiss-Prot/UniProt ID: P05121

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1. Courey AJ, Horowitz JC, Kim KK et-al. The vitronectin-binding function of PAI-1 exacerbates lung fibrosis in mice. Blood. 2011;118 (8): 2313-21. doi:10.1182/blood-2010-12-324574Free text at pubmedPubmed citation

2. Wan YZ, Gao P, Zhou S, et al. SIRT1-mediated epigenetic downregulation of plasminogen activator inhibitor-1 prevents vascular endothelial replicative senescence. Aging Cell. 2014;13(5):890-9. Link to article