Cyclophilin E/PPIase E/PPIE Protein(N-6His) (recombinant human)

Protein Construction: Recombinant Human Peptidyl-Prolyl cis-trans Isomerase E is produced by our E.coli expression system and the target gene encoding Met1-Val301 is expressed with a 6His tag at the N-terminus. Sequence: Met 1-Val301. Fusion tag: N-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 34 kDa. Protein function: Peptidyl-prolyl cis-trans isomerase E, also known as Cyclophilin E, Cyclophilin-33, Rotamase E, CYP33, PPIE, is an enzyme which belongs to the cyclophilin-type PPIase family of PPIase E subfamily. PPIE found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. PPIE contains one PPIase cyclophilin-type domain and one RRM (RNA recognition motif) domain. PPIE accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIE combines RNA-binding and PPIase activities. It may be involved in muscle- and brain-specific processes and pre-mRNA splici Protein function: Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28076346). Combines RNA- binding and PPIase activities (PubMed:8977107, PubMed:18258190, PubMed:20677832, PubMed:20460131). Binds mRNA and has a preference for single-stranded RNA molecules with poly-A and poly-U stretches, suggesting it binds to the poly(A)-region in the 3'-UTR of mRNA molecules (PubMed:8977107, PubMed:18258190, PubMed:20460131). Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins (PubMed:8977107, PubMed:18258190, PubMed:20677832, PubMed:20541251). Inhibits KMT2A activity, this requires proline isomerase activity (PubMed:20677832, PubMed:20541251, PubMed:20460131). [The UniProt Consortium]