Human PAI-1 (stable mutant, no LRP binding)
A substitution of Glutamic Acid for Arginine at position 76 greatly decreases the binding of this Human PAI-1 mutant to the low density lipoprotein receptor-related protein (LRP). The putative LRP binding exosite is thought to overlap with the heparin binding site on the PAI-1 molecule. Binding to LRP or similar receptors leads to the clearance of PAI-1 complexes. An additional mutation (Isoleucine 91 to Leucine) provides increased stability for use in long term binding experiments or in vivo studies. A human PAI-1 point mutation stable form (Catalog Number HPAI-I91L) is available as an LRP binding control PAI-1.
Stefansson S. et al. (1998) J Biol Chem 273:6358-6366.