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Product Description
Cyclophilins possess the activity of peptidyl-prolyl cis-trans isomerase (PPIase) and are involved in cellular protein folding and protein interactions. PPIE contains two RNA binding domains at the N-terminal region and a PPIase domain at the C-terminal region. The cellular and physiological roles of PPIE are still not known.
Biovision | 6314 | Human Recombinant Cyclophilin E DataSheet
Biomolecule/Target: N/A
Synonyms: Human Recombinant Cyclophilin E
Alternates names: Peptidylprolyl isomerase E isoform 1, PPIE, CYP-33, Cyclophilin E, PPIase E, Rotamase E
Taglines: An immunophilin family protein catalyzing the isomerization of peptide bonds
NCBI Gene ID #: 332
NCBI Gene Symbol: BIRC5
Gene Source: Human
Accession #: O15392
Recombinant: Yes
Source: E. coli
Purity by SDS-PAGEs: 90%
Assay: SDS-PAGE
Purity: N/A
Assay #2: N/A
Endotoxin Level: N/A
Activity (Specifications/test method): N/A
Biological activity: Specific activity is > 210 nmoles/min/mg
Results: N/A
Binding Capacity: N/A
Unit Definition: Specific activity is defined as the amount of enzyme that cleaves 1 µmole of Suc-AAFP-pNA per minute at 25°C in Tris HCl pH 8.0 using chymotrypsin.
Molecular Weight: 37.5 kDa
Concentration: 1 mg/ml
Appearance: Liquid
Physical form description: 1 mg/ml solution in 20 mM Tris-HCl buffer (pH 8.0)
Reconstitution Instructions: N/A
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
