PAI-1 mutant stable, 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.

References:
Stefansson S. et al.1998 J Biol Chem 273:6358-6366.

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Transport temperature: Dry ice
Supplier: Molecular Innovations