Peptidyl-prolyl Cis-trans Isomerase D

E6692Hu

Sandwich

48T,96T

0.013ng/ml

0.05-15ng/ml

Serum, plasma, cell culture supernates

Human

2-8ºC

1h 30m

PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:11350175, PubMed:20676357). Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large-cell lymphoma (ALK+ ALCL) cell lines. (Microbial infection) May be involved in hepatitis C virus (HCV) replication and release.

40,764

5481

40 kDa peptidyl-prolyl cis-trans isomerase;Cyclophilin-40;Cyclophilin-related protein;CYP-40;CYPD;Peptidyl-prolyl cis-trans isomerase D;PPIase D;Rotamase D

PPID

Immunology

Cyclophilin-40