Recombinant Human Cyclophilin E/PPIE Protein (His Tag) (PKSH032317)
For research use only.
| Synonyms | CYP33, Cyclophilin E, Cyclophilin-33, PPIE, PPIase E, Peptidyl-Prolyl Cis-Trans Isomerase E, Rotamase E |
| Species | Human |
| Expression Host | E.coli |
| Sequence | Met 1-Val301 |
| Accession | Q9UNP9 |
| Calculated Molecular Weight | 35.6 kDa |
| Observed Molecular Weight | 34 kDa |
| Tag | N-His |
| Bio-activity | Not validated for activity |
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles. |
| Shipping | This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at < - 20°C. |
| Formulation | Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, pH 8.0. |
| Reconstitution | Not Applicable |
| Background | 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 |
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