A portion of amino acids 336-370 from the human protein was used as the immunogen for the Cyclophilin D antibody.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. 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. May be involved in hepatitis C virus (HCV) replication and release.
Western blot: 1:500-1:2000,Flow cytometry: 1:25 (1x10e6 cells),Immunohistochemistry (FFPE): 1:25,Immunofluorescence: 1:25
Anwendungsbeschreibung:
The stated application concentrations are suggested starting points. Titration of the Cyclophilin D antibody may be required due to differences in protocols and secondary/substrate sensitivity.
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