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PFDN5 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q99471 |
|---|---|
| Clone Names | 100324077 |
| Gene ID | 5204 |
|---|---|
| Other Names | Prefoldin subunit 5, C-Myc-binding protein Mm-1, Myc modulator 1, PFDN5, MM1, PFD5 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP13122c was selected from the Center region of PFDN5. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | PFDN5 |
|---|---|
| Synonyms | MM1, PFD5 |
| Function | Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC. |
| Cellular Location | [Isoform 1]: Nucleus. [Isoform 3]: Nucleus. |
| Tissue Location | Highly expressed in pancreas and skeletal muscle and moderately in other tissues |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a member of the prefoldin alpha subunitfamily. The encoded protein is one of six subunits of prefoldin, amolecular chaperone complex that binds and stabilizes newlysynthesized polypeptides, thereby allowing them to fold correctly.The complex, consisting of two alpha and four beta subunits, formsa double beta barrel assembly with six protruding coiled-coils. Theencoded protein may also repress the transcriptional activity ofthe proto-oncogene c-Myc. Alternatively spliced transcript variantsencoding different isoforms have been described. [provided byRefSeq].
References
Ma, H.C., et al. J. Biomed. Sci. 15(4):417-425(2008)Yoshida, T., et al. Exp. Cell Res. 314(6):1217-1228(2008)Lubyova, B., et al. J. Biol. Chem. 282(44):31944-31953(2007)Hagio, Y., et al. J. Cell. Biochem. 97(1):145-155(2006)Bruneel, A., et al. Proteomics 5(15):3876-3884(2005)
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