Cyclophilin-E is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-E contains a highly conserved cyclophilin domain in addition to a RNA-binding domain. Cyclophilin-E exhibits PPIase activity, protein folding activities and possess RNA-binding activity. Cyclophilin-E contains 2 RNA binding domains at the N-terminal region and a PPIase domain at the C-terminal region.
Cyclophilin-E Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 337 amino acids (1-301 a.a.) and having a molecular mass of 37.5 kDa. Cyclophilin-E is fused to 36 amino acids long His Tag at N-terminus and is purified by proprietary chromatographic techniques.