Anti-PPID Antibody Picoband® fluoro594 Vervoeging

Cyclophilin D, Peptidylprolyl isomerase D, also known as PPID, is an enzyme which in humans is encoded by the PPID gene. The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. The Cyclophilin D (PPID) gene contains 10 exons and spans 14.2 kb of genomic DNA. By fluorescence in situ hybridization, the PPID gene is mapped to chromosome 4q31.3. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein has been shown to possess PPIase activity and, similar to other family members, can bind to the immunosuppressant ciclosporin.

Peptidyl-prolyl cis-trans isomerase D; PPIase D;5.2.1.8;40 kDa peptidyl-prolyl cis-trans isomerase; Cyclophilin-40; CYP-40; Cyclophilin-related protein; Rotamase D; PPID; CYP40, CYPD

PPID

5481

Q08752

Human, Mouse, Rat

No cross-reactivity with other proteins

A synthetic peptide corresponding to a sequence at the C-terminus of human PPID, different from the related mouse and rat sequence by one amino acid.

Widely expressed.

Flow Cytometry

Cardiovascular, Immunology

Immunogen affinity purified.

Liquid

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. .

1. Kieffer, L. J., Thalhammer, T., Handschumacher, R. E.Isolation and characterization of a 40-kDa cyclophilin-related protein.J. Biol. Chem. 267: 5503-5507, 1992. 2. Ratajczak, T., Woollatt, E., Kumar, P., Ward, B. K., Minchin, R. F., Baker, E.Cyclophilin 40 (PPID) gene map position 4q31.3.Chromosome Res. 5: 151 only, 1997. 3. Yokoi, H., Shimizu, Y., Anazawa, H., Lefebvre, C. A., Korneluk, R. G., Ikeda, J.-E.The structure and complete nucleotide sequence of the human cyclophilin 40 (PPID) gene.Genomics 35: 448-455, 1996.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

40764 MW

No cross reactivity with other proteins.

6

Peptidyl-prolyl cis-trans isomerase D

Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm.

Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.

Peptidyl-prolyl cis-trans isomerase D (PPIase D)

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.