Product Pathways - Chromatin Regulation / Epigenetics
Phospho-SirT1 (Ser27) Antibody #2327
|2327L||300 µl (30 western blots)||---||In Stock||---|
|2327S||100 µl (10 western blots)||---||In Stock||---|
|2327||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
This antibody detects endogenous levels of SirT1 protein only when phosphoryated on serine 27. The antibody does not cross-react with other sirtuin proteins.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser27 of human SirT1. Antibodies are purified by protein A and peptide affinity chromatography.
The Silent Information Regulator (SIR2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as class III histone deacetylases. The first discovered and best characterized of these genes is Saccharomyces cerevisiae SIR2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (1). SirT1, the mammalian ortholog of Sir2, is a nuclear protein implicated in the regulation of many cellular processes, including apoptosis, cellular senescence, endocrine signaling, glucose homeostasis, aging, and longevity. Targets of SirT1 include acetylated p53 (2,3), p300 (4), Ku70 (5), forkhead (FoxO) transcription factors (5,6), PPARγ (7), and the PPARγ coactivator-1α (PGC-1α) protein (8). Deacetylation of p53 and FoxO transcription factors represses apoptosis and increases cell survival (2,3,5,6). Deacetylation of PPARγ and PGC-1α regulates the gluconeogenic/glycolytic pathways in the liver and fat mobilization in white adipocytes in response to fasting (7,8). SirT1 deacetylase activity is inhibited by nicotinamide and activated by resveratrol. In addition, SirT1 activity may be regulated by phosphorylation, as it is phosphorylated at Ser27 and Ser47 in vivo; however, the function of these phosphorylation sites has not yet been determined (9).
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- Bouras, T. et al. (2005) J. Biol. Chem. 280, 10264-10276.
- Brunet, A. et al. (2004) Science 303, 2011-2015.
- Motta, M.C. et al. (2004) Cell 116, 551-563.
- Picard, F. et al. (2004) Nature 429, 771-776.
- Rodgers, J.T. et al. (2005) Nature 434, 113-118.
- Beausoleil, S.A. et al. (2004) Proc. Natl. Acad. Sci. USA 101, 12130-12135.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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