Peptidyl-prolyl cis-trans isomerase E (PPIE) is a cyclophilin which binds to RNA. It contains a conserved PPIase (peptidylprolyl isomerase) domain and a RNA-binding motif.
Synonyms: Anti-Cyclophilin E; Anti-Cyclophilin-33; Anti-PPIase E; Anti-Peptidyl-prolyl cis-trans isomerase E; Anti-Rotamase E
Storage: -20C
Application: All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry. The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: Peptidyl-prolyl cis-trans isomerase E (PPIE) is involved in the cis-trans isomerization of the peptide bond before a proline residue. It facilitates conformational changes in folded and unfolded proteins. PPIE also mediates protein interactions and transport. PPIE recruits histone deacetylases to mixed lineage leukemia (MLL) genes and functions in down-regulating the target proteins like homeobox C8 (HOXC8). Studies have shown that it binds to influenza A virus nucleoprotein and prevents viral replication.
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