|Other Names||Peptidyl-prolyl cis-trans isomerase E, PPIase E, Cyclophilin E, Cyclophilin-33, Rotamase E, PPIE, CYP33|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Tissue Location||Found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas|
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The protein encoded by this gene is a member of thepeptidyl-prolyl cis-trans isomerase (PPIase) family. PPIasescatalyze the cis-trans isomerization of proline imidic peptidebonds in oligopeptides and accelerate the folding of proteins. Thisprotein contains a highly conserved cyclophilin (CYP) domain aswell as an RNA-binding domain. It was shown to possess PPIase andprotein folding activities, and it also exhibits RNA-bindingactivity. Alternative splicing results in multiple transcriptvariants. A related pseudogene, which is also located on chromosome1, has been identified.
Park, S., et al. Biochemistry 49(31):6576-6586(2010)Hom, R.A., et al. J. Mol. Biol. 400(2):145-154(2010)Wang, Z., et al. Cell 141(7):1183-1194(2010)Naukkarinen, J., et al. PLoS Genet. 6 (6), E1000976 (2010) :Chen, J., et al. Cancer Res. 68(15):6199-6207(2008)
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