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PPIE Protein, Human, Recombinant (His)

Catalog No. TMPJ-01389

Peptidyl-prolyl cis-trans isomerase E, also known as Cyclophilin E, Cyclophilin-33, Rotamase E, CYP33, PPIE, is an enzyme which belongs to the cyclophilin-type PPIase family of PPIase E subfamily. PPIE found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. PPIE contains one PPIase cyclophilin-type domain and one RRM (RNA recognition motif) domain. PPIE accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIE combines RNA-binding and PPIase activities. It may be involved in muscle- and brain-specific processes and pre-mRNA splici

PPIE Protein, Human, Recombinant (His)

PPIE Protein, Human, Recombinant (His)

Catalog No. TMPJ-01389
Peptidyl-prolyl cis-trans isomerase E, also known as Cyclophilin E, Cyclophilin-33, Rotamase E, CYP33, PPIE, is an enzyme which belongs to the cyclophilin-type PPIase family of PPIase E subfamily. PPIE found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. PPIE contains one PPIase cyclophilin-type domain and one RRM (RNA recognition motif) domain. PPIE accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIE combines RNA-binding and PPIase activities. It may be involved in muscle- and brain-specific processes and pre-mRNA splici
Pack SizePriceAvailabilityQuantity
10 μg$1847-10 days
50 μg$5457-10 days
500 μg$1,9007-10 days
1 mg$2,7307-10 days
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Product Information

Biological Activity
Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description
Peptidyl-prolyl cis-trans isomerase E, also known as Cyclophilin E, Cyclophilin-33, Rotamase E, CYP33, PPIE, is an enzyme which belongs to the cyclophilin-type PPIase family of PPIase E subfamily. PPIE found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. PPIE contains one PPIase cyclophilin-type domain and one RRM (RNA recognition motif) domain. PPIE accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIE combines RNA-binding and PPIase activities. It may be involved in muscle- and brain-specific processes and pre-mRNA splici
Species
Human
Expression System
E. coli
TagN-6xHis
Accession NumberQ9UNP9
Synonyms
Rotamase E,PPIE,PPIase E,Peptidyl-Prolyl Cis-Trans Isomerase E,CYP33,Cyclophilin-33,Cyclophilin E
Amino Acid
Met1-Val301
Construction
Met1-Val301
Protein Purity
Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight34 KDa (reducing condition)
Endotoxin< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
FormulationSupplied as a 0.2 μm filtered solution of 20 mM Tris-HCl, pH 8.0.
Stability & Storage
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
ShippingShipping with blue ice.
Research Background
Peptidyl-prolyl cis-trans isomerase E, also known as Cyclophilin E, Cyclophilin-33, Rotamase E, CYP33, PPIE, is an enzyme which belongs to the cyclophilin-type PPIase family of PPIase E subfamily. PPIE found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. PPIE contains one PPIase cyclophilin-type domain and one RRM (RNA recognition motif) domain. PPIE accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIE combines RNA-binding and PPIase activities. It may be involved in muscle- and brain-specific processes and pre-mRNA splici

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