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Our customer service representatives are available 24 hours, Monday through Friday to assist you.| Introduction | 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. |
| Synonyms | Peptidyl-prolyl cis-trans isomerase E, PPIase E, Rotamase E, Cyclophilin-33, PPIE, peptidylprolyl isomerase E, CYP33, Cyclophilin E, CYP-33, MGC3736, MGC111222. |
| Source | Escherichia Coli. |
| Physical Appearance | Sterile filtered colorless solution. |
| Formulation | Cyclophilin-E solution containing 20mM Tris pH-8. |
| Stability | Cyclophilin-E Human Recombinant althoµgh stable at 4°C for 1 week, should be stored below -18°C. Please prevent 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 QF |
| Purity | Greater than 95.0% as determined by SDS-PAGE. |
| Biological Activity | Specific activity is > 210 nmoles/min/µg, 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. |
| Usage | NeoBiolab's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drµgs, agricultural or pesticidal products, food additives or household chemicals. |
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