Prefoldin subunit 5 (PFDN5) is a heterohexameric chaperone protein that is present in the nucleus. The gene encoding it is present on chromosome 12q12-12q13. PFDN5 is a subunit of prefoldin/Gim, which is a chaperon protein complex involved in sorting unfolded proteins to a chaperonin.
Synonyms: Anti-C-myc-binding protein Mm-1 antibody produced in rabbit; Anti-Myc modulator 1 antibody produced in rabbit; Anti-Prefoldin subunit 5 antibody produced in rabbit
Storage: -20C
Application: All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry. The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: Prefoldin subunit 5 (PFDN5) binds to cytosolic chaperonin (c-cpn) and transfers target proteins to it. It also binds to nascent polypeptide chains and promotes folding. PFDN5 recognizes only non-native proteins but not native and aggregated proteins. It binds to the myc box II, which is present in the transactivation domain of c-Myc and represses the E-box-dependent transcriptional activity of c-Myc. For this repression, PFDN5 directly binds to transcriptional intermediary factor 1ß (TIF1ß), which is a transcriptional corepressor and recruits an histone deacetylase (HDAC) complex.
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