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Questions? Please consult our answers to frequently asked questions at http://www.ebioscience.com/faq. DescriptionThis is a peptide mapping to the carboxy terminal domain of human SIRT1. The Sir2 protein in yeast is known to function in transcriptional silencing processes through the deacetylation of histones H3 and H4 (1). The more recently described human homologue of Sir2, known as SIRT1, has been found to associate with the tumor suppressor protein p53 (1-3). SIRT1 binds and deacetylates p53 with specificity for its C-terminal Lys382 residue in response to the upregulation of promyelocytic leukemia protein (PML) nuclear bodies or oncogenic Ras (2&3). The deacetylation of p53 SIRT1 has been shown to negatively regulate p53-mediated transcription, preventing cellular senescence and apoptosis induced by DNA damage and stress (1-3). Applications ReportedFor research use only, not for diagnostic or therapeutic use. This blocking peptide has been reported for use in competition studies. References
1. Smith J. 2002. Human Sir2 and the 'silencing' of p53 activity. Trends Cell Biol. 12(9):404-406. 2. Vaziri H, Dessain SK, Ng Eaton E, Imai SI, Frye RA, Pandita TK, Guarente L, Weinberg RA. 2001. HSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 107(2):149-159. 3. Langley E, Pearson M, Faretta M, Bauer UM, Frye RA, Minucci S, Pelicci PG, Kouzarides T. 2002. Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J. 21(10):2383-2396. Related ProductsCat. 14-6769 Purified anti-human SIRT1 polyclonal (clone Polyclonal) |
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