Ppid (NM_026352) Mouse Recombinant Protein
SKU
TP505715
Purified recombinant protein of Mouse peptidylprolyl isomerase D (cyclophilin D) (Ppid), with C-terminal MYC/DDK tag, expressed in HEK293T cells, 20ug
$1,020.00
4 Weeks*
Specifications
| Product Data | |
| Species | Mouse |
|---|---|
| Expression Host | HEK293 |
| Expression cDNA Clone or AA Sequence | |
| Tag | C-MYC/DDK |
| Predicted MW | 41.2 kDa |
| Concentration | >0.05 µg/µL as determined by microplate BCA method |
| Purity | > 80% as determined by SDS-PAGE and Coomassie blue staining |
| Buffer | 25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol |
| Note | For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process. |
| Storage | Store at -80°C after receiving vials. |
| Stability | Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles. |
| Shipping | Dry Ice |
| Reference Data | |
| RefSeq | NP_080628 |
| Locus ID | 67738 |
| UniProt ID | Q9CR16 |
| Cytogenetics | 3 E3 |
| RefSeq Size | 1728 |
| RefSeq ORF | 1110 |
| Synonyms | 4930564J03Rik; CYP-40; Ppidl; Ppif |
| Summary | PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. 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 region. Involved in regulation of UV radiation-induced apoptosis.UniProtKB/Swiss-Prot Function |
| Protein Categories | Intracellular Proteins |
Reviews
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Resources
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Citations
*Delivery time may vary from web posted schedule. Occasional delays may occur due to unforeseen
complexities in the preparation of your product. International customers may expect an additional 1-2 weeks
in shipping.
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