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The protein encoded by PPIE is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. Additionally we are shipping Peptidylprolyl Isomerase E (Cyclophilin E) Antibodies (61) and many more products for this protein.
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Human PPIE Protein expressed in Escherichia coli (E. coli) - ABIN667726
Mi, Kops, Zimmermann, Jäschke, Tropschug: A nuclear RNA-binding cyclophilin in human T cells. in FEBS letters 1997
Show all 2 references for ABIN667726
A new family of cyclophilins with an RNA recognition motif that interact with members of the trx (show GSR Proteins)/MLL (show MLL Proteins) protein family in Drosophila and human cells.
CypE is a host restriction factor that inhibits the functions of nucleoprotein, as well as viral replication and transcription, by impairing the formation of the viral ribonucleoprotein complex.
binding of H3K4me3 to PHD3 (show EGLN3 Proteins) domain of MLL (show MLL Proteins) and binding of the CYP33 RRM domain to PHD3 (show EGLN3 Proteins) are mutually inhibitory, implying that PHD3 (show EGLN3 Proteins) is a molecular switch for the transition between activation and repression of target genes
PPIase (show FKBP1B Proteins) domain of CyP33 regulates the conformation of MLL1 through proline isomerization within the PHD3 (show EGLN3 Proteins)-Bromo linker, thereby disrupting the PHD3 (show EGLN3 Proteins)-Bromo interface and facilitating binding of the MLL1-PHD3 (show EGLN3 Proteins) domain to the CyP33-RRM domain.
Data provide insight into the multiple functions of Cyp33 RRM and suggest a Cyp33-dependent mechanism for regulating the transcriptional activity of MLL (show MLL Proteins).
The results show that hCyP33 binds specifically to mRNA, namely poly(A)(+)RNA, and that binding stimulates the PPIase (show FKBP1B Proteins) activity of hCyP33.
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.
, peptidyl-prolyl cis-trans isomerase E
, peptidylprolyl isomerase E (cyclophilin E)
, peptidylprolyl isomerase E
, cyclophilin E
, PPIase E
, rotamase E