The Human (CYCLOPHILIN-40) Peptidyl-prolyl Cis-Trans Isomerase D ELISA Kit measures Peptidyl-prolyl Cis-trans Isomerase D in samples. The plate has been pre-coated with Human Cyclophilin-40 antibody. Cyclophilin-40 present in the sample is added and binds to antibodies coated on the wells. And then biotinylated Human Cyclophilin-40 Antibody is added and binds to Cyclophilin-40 in the sample. Then Streptavidin-HRP is added and binds to the Biotinylated Cyclophilin-40 antibody. After incubation unbound Streptavidin-HRP is washed away during a washing step. Substrate solution is then added and color develops in proportion to the amount of Human Cyclophilin-40. The reaction is terminated by addition of acidic stop solution and absorbance is measured at 450 nm.
BackgroundPPIase 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. Source: UniProt Consortium (2025)
