Cyclophilin E Human

Cyclophilin-E is characterized by its ability to accelerate the folding of proteins by catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides . This enzyme combines RNA-binding and PPIase activities, which suggests its involvement in muscle- and brain-specific processes as well as pre-mRNA splicing .

Cyclophilin-E is found in various tissues, including the heart, brain, placenta, lung, liver, skeletal muscle, kidney, and pancreas . This widespread distribution indicates its essential role in numerous physiological processes.

Recombinant human Cyclophilin-E is typically produced in E. coli expression systems. The recombinant protein is often tagged with a His-tag for purification purposes . The molecular weight of the recombinant protein is approximately 35.6 kDa .

Cyclophilin-E has been extensively studied for its role in protein folding and its potential involvement in various cellular processes. It is also known for being a target of the immunosuppressive drug cyclosporin, which is used to prevent organ transplant rejection . The structural and biochemical characterization of Cyclophilin-E and other cyclophilins is crucial for understanding their substrate specificity and for the development of isoform-selective ligands .

Recombinant human Cyclophilin-E is typically supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, pH 8.0. It should be stored at temperatures below -20°C to ensure stability and minimize freeze-thaw cycles .

Cyclophilin-E’s multifaceted roles and its importance in various biological processes make it a significant subject of study in the field of biochemistry and molecular biology.