Cell Signaling Technology

Product Pathways - Chromatin Regulation / Epigenetics

SirT1 Antibody #2310

Applications Reactivity Sensitivity MW (kDa) Source
W H Endogenous 120 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

SirT1 antibody detects endogenous levels of total SirT1 protein. The antibody does not cross-react with other sirtuin proteins.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus of human SirT1. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of lysates from 293, HCT15 and RD-ES cells, using SirT1 Antibody.

Background

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, since it is phosphorylated on Ser27 and Ser47 in vivo, however, the function of these phosphorylation sites has not yet been determined (9).

  1. Guarente, L. (1999) Nat. Genet. 23, 281-285.
  2. Vaziri, H. et al. (2001) Cell 107, 149-159.
  3. Luo, J. et al. (2001) Cell 107, 137-148.
  4. Bouras, T. et al. (2005) J. Biol. Chem. 280, 10264-10276.
  5. Brunet, A. et al. (2004) Science 303, 2011-2015.
  6. Motta, M.C. et al. (2004) Cell 116, 551-563.
  7. Picard, F. et al. (2004) Nature 429, 771-776.
  8. Rodgers, J.T. et al. (2005) Nature 434, 113-118.
  9. Beausoleil, S.A. et al. (2004) Proc. Natl. Acad. Sci. USA 101, 12130-12135.

Application References

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Companion Products

This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.

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