SirT1 (C14H4) Rabbit mAb #2496
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 120 |
| Source/Isotype | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:25 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
SirT1 (C14H4) Rabbit mAb detects endogenous levels of total SirT1 protein. This antibody does not cross-react with other sirtuin proteins.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus of the human SirT1 protein.
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, as it is phosphorylated at Ser27 and Ser47 in vivo; however, the function of these phosphorylation sites has not yet been determined (9).
- Guarente, L. (1999) Nat. Genet. 23, 281-285.
- Vaziri, H. et al. (2001) Cell 107, 149-159.
- Luo, J. et al. (2001) Cell 107, 137-148.
- 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.
- Kozako, T. et al. (2015) Sci Rep 5, 11345.
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