Cyclophilin E Active Protein | PPIE active protein

Human Recombinant Cyclophilin E

Cat. Num. AAA845370

• Gene Names: PPIE; CYP33; CYP-33
• Applications: SDS-Page
• Purity: >=95%
• Synonyms: Cyclophilin E; Human Recombinant Cyclophilin E; Peptidylprolyl isomerase E isoform 1; PPIE; CYP-33; PPIase E; Rotamase E; PPIE active protein

• Host: E Coli
• Purity/Purification: >=95%
• Form/Format: 1 mg/ml solution in 20 mM Tris-HCl buffer (pH 8.0); Appearance: Liquid
• Concentration: 1 mg/ml (varies by lot)
• 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
• Sequence Length: 314

• Applicable Applications for PPIE active protein: SDS-PAGE
• Biological Activity: Specific activity is > 210 nmoles/min/mg
• Unit Definition: Specific activity is defined as the amount of enzyme that cleaves 1 umole of Suc-AAFP-pNA per minute at 25 degree C in Tris HCl pH 8.0 using chymotrypsin.
• Handling: Centrifuge the vial prior to opening.
• Preparation and Storage: At -80 degree C; Shelf Life: 12 months

Testing Data

Related Product Information for PPIE active protein

Background: 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.

Product Categories/Family for PPIE active protein

Proteins and Enzymes; Proteins and Enzymes (A-Z)  

NCBI and Uniprot Product Information

• NCBI GI #: 303305009
• NCBI GeneID: 10450
• NCBI Accession #: NP_001181936.1
• NCBI GenBank Nucleotide #: NM_001195007.1
• UniProt Accession #: Q9UNP9; O43634; O43635; Q32Q72; Q3S611; Q5TGA0; Q5TGA2; Q5TGA3; Q9UIZ5; B2R971
• Molecular Weight: 37.5 kDa
• NCBI Official Full Name: peptidyl-prolyl cis-trans isomerase E isoform 4
• NCBI Official Synonym Full Names: peptidylprolyl isomerase E (cyclophilin E)
• NCBI Official Symbol: PPIE
• NCBI Official Synonym Symbols: CYP33; CYP-33
• NCBI Protein Information: peptidyl-prolyl cis-trans isomerase E
• UniProt Protein Name: Peptidyl-prolyl cis-trans isomerase E
• UniProt Gene Name: PPIE
• UniProt Synonym Gene Names: CYP33; PPIase E
• UniProt Entry Name: PPIE_HUMAN

NCBI Description

The protein encoded by this gene 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 accelerate the folding of proteins. This protein contains a highly conserved cyclophilin (CYP) domain as well as an RNA-binding domain. It was shown to possess PPIase and protein folding activities, and it also exhibits RNA-binding activity. Alternative splicing results in multiple transcript variants. A related pseudogene, which is also located on chromosome 1, has been identified. [provided by RefSeq, Aug 2010]

Uniprot Description

PPIE: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing. Belongs to the cyclophilin-type PPIase family. PPIase E subfamily. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 5.2.1.8; Spliceosome; Cyclophilin; RNA splicing; Isomerase

Chromosomal Location of Human Ortholog: 1p32

Cellular Component: nucleus

Molecular Function: protein binding; peptidyl-prolyl cis-trans isomerase activity; RNA binding; nucleotide binding; cyclosporin A binding

Biological Process: nuclear mRNA splicing, via spliceosome; positive regulation of viral genome replication; protein peptidyl-prolyl isomerization; regulation of transcription, DNA-dependent; protein folding