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Cyclophilin D Antibody
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, FC, IHC-P, IF, E |
|---|---|
| Primary Accession | Q08752 |
| Other Accession | Q9CR16, Q6DGG0 |
| Reactivity | Human |
| Predicted | Mouse, Rat |
| Host | Rabbit |
| Clonality | polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 40764 Da |
| Gene ID | 5481 |
|---|---|
| Other Names | 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 |
| Target/Specificity | This Cyclophilin D antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 336-370 amino acids from the human region of human Cyclophilin D. |
| Dilution | IF~~1:25 WB~~1:2000 IHC-P~~1:25 FC~~1:25 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Cyclophilin D Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | PPID (HGNC:9257) |
|---|---|
| Synonyms | CYP40, CYPD |
| Function | 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. |
| Cellular Location | Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm |
| Tissue Location | Widely expressed. |
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
Kieffer L.J.,et al.J. Biol. Chem. 268:12303-12310(1993).
Yokoi H.,et al.Genomics 35:448-455(1996).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
Gevaert K.,et al.Nat. Biotechnol. 21:566-569(2003).
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