Cyclophilin E Recombinant Protein
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| Amount : | 25 µg |
| Purification : | Greater than 95.0% as determined by SDS-PAGE. |
| Content : | Cyclophilin-E solution containing 20mM Tris pH-8. |
| Storage condition : | Cyclophilin-E Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles. |
| AA 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. |
| Alternative Name : | 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.
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.
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.
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.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
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