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Cyclophilin-E Human Recombinant ( Cyclophilin E Human )
DescriptionCyclophilin-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
Data sheet
| Formulation | Cyclophilin-E solution containing 20mM Tris pH-8. |
| Purity | Greater than 95.0% as determined by SDS-PAGE. |
| Description | 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 a 36 amino acids long His Tag at N-terminus and is purified by proprietary chromatographic techniques. |
| Protein Background | 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. |
| Expression host | Escherichia Coli. |
| Synonyms | Peptidyl-prolyl cis-trans isomerase E, PPIase E, Rotamase E, Cyclophilin-33, PPIE, peptidylprolyl isomerase E, CYP33, Cyclophilin E, CYP-33, MGC3736, MGC111222. |
| Reagent Appearance | Sterile filtered colorless solution. |
| Stability | Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. |
| Amino acid sequence | MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMATT KRVLYVGGLA EEVDDKVLHA AFIPFGDITD IQIPLDYETE KHRGFAFVEF ELAEDAAAAI DNMNESELFG RTIRVNLAKP MRIKEGSSRP VWSDDDWLKK FSGKTLEENK EEEGSEPPKA ETQEGEPIAK KARSNPQVYM DIKIGNKPAG RIQMLLRSDV VPMTAENFRC LCTHEKGFGF KGSSFHRIIP QFMCQGGDFT NHNGTGGKSI YGKKFDDENF ILKHTGPGLL SMANSGPNTN GSQFFLTCDK TDWLDGKHVV FGEVTEGLDV LRQIEAQGSK DGKPKQKVII ADCGEYV. |
| Biological Activity | Specific activity is > 210 nmoles/min/ug, and is defined as the amount of enzyme that cleave 1umole of suc-AAFP-pNA per minute at 1C in Tris-HCl pH8.0 using chymotrypsin. |