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

$695$1,140

Clear
SKU: HPAI-RR Categories: ,

Product Description

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.
References
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

View sample datasheet
View sample certificate of analysis
View material safety data sheet
Ask a question about this product

Additional Information

Purity

Source

Molecular Weight

Extinction Coefficient

Species

Storage

Shipping Conditions

Expiration

Form

Buffer

Sample Size

Sample Concentration

Sample Volume

Gene Name

Gene ID

UniProt ID

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