10011190  SIRT1 (human recombinant)

Silent Information Regulator 2; Sirtuin 1; Sir 2

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• See more Enzyme Activity; High Throughput Screening; Inhibitor Screening Assay; Western Blot; Enzymes; Histone Deacetylase; Proteins; Recombinant Proteins; Apoptosis; Cancer; Chromatin Research; Epigenetics; Histone Modification

For active pharmaceutical ingredients (APIs) related to SIRT1 (human recombinant), see Cayman Pharma

Source: recombinant N-terminal GST-tagged SIRT1 amino acids 193-747 purified from E. coli · Mr: 89.2 kDa · The sirtuins represent a distinct class of trichostatin A-insensitive lysyl-deacetylases (class III HDACs) and have been shown to catalyze a reaction that couples lysine deacetylation to the formation of nicotinamide and O-acetyl-ADP-ribose from NAD+ and the abstracted acetyl group.1,2,3 There are seven human sirtuins, which have been designated SIRT1-7.4 SIRT1, which is located in the nucleus, is the human sirtuin with the greatest homology to yeast Sir2 (Silent information regulator 2) and has been shown to regulate the activity of the p53 tumor suppressor and inhibit apoptosis.5,6,7 These results have significant implications regarding an important role of SIRT1 in modulating the sensitivity of cells in the p53-dependent apoptotic response and the possible effect in cancer therapy. Since the growth suppressive function of p53 is strongly enhanced by DNA damaging reagents, it is expected that inhibitors of SIRT1 may be effective anti-cancer drugs.8
1  Imai, S., Armstrong, C.M., Kaeberlein, M., et al. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403 795-800 (2000).
2  Tanner, K.G., Landry, J., Sternglanz, R., et al. Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc Natl Acad Sci USA 97(26) 14178-14182 (2000).
3  Tanny, J.C., Moazed, D. Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product. Proc Natl Acad Sci USA 98(2) 415-420 (2001).
4  Frye, R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 273 793-798 (2000).
5  Luo, J., Nikolaev, A.Y., Imai, S., et al. Negative control of p53 by Sir2α promotes cell survival under stress. Cell 107 137-148 (2001).
6  Vaziri, H., Dessain, S.K., Eaton, E.N., et al. hSIR2SIRT1 functions as an NAD-dependent p53 deacetylase. Cell 107 149-159 (2001).
7  Langley, E., Pearson, M., Faretta, M., et al. Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J 21(10) 2383-2396 (2002).
8  Longo, V.D., Kennedy, B.K. Sirtuins in aging and age-related disease. Cell 126 257-268 (2006).

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Pricing Information

Prices listed here are the Manufacturer's Suggested European Retail Price. The actual prices quoted by each individual distributor may vary. Please visit the Global Buyer's Guide on the Cayman Chemical (world) website to locate a distributor in your region.

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Size Price Quantity
25 units €115.00
50 units €218.00
100 units €411.00
Pricing updated 2010-03-11.
Prices are subject to change without notice.