Purified human recombinant enzyme
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SIRT6 (human, recombinant)

Item No. 10315

Product Insert (PDF)
Technical Information
Synonyms
  • NAD-dependent Deacetylase 6
  • Silent Information Regulator 6
  • SIR2L6
  • SIR2-like Protein 6
  • Sirtuin 6
Purity
≥80% estimated by SDS-PAGE
Source
active recombinant N-terminal His-tagged enzyme expressed in E. coli
Amino Acids
1-355
MW
43.7 kDa
25 mM Tris-HCl, pH 8.0, with 100mM NaCl, 20% glycerol
UniProt Accession №
Q8N6T7
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    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 SIRT6 associates specifically with telomeres and functions at chromatin to decrease NF-κB signaling.5,6 Mammalian cells depleted of SIRT6 display abnormal telomere structures similar to defects found in Werner syndrome, a premature ageing disorder, and have a shortened life span.5,6 Since SIRT6 binds and attenuates NF-κB signaling, it is proposed that activators of SIRT6 may be effective anti-cancer and anti-inflammatory drugs and may increase longevity.5

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Imai, S.I., Armstrong, C.M., Kaeberlein, M., et alTranscriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403(6771), 795-800 (2000).

    2. Tanner, K.G., Landry, J., Sternglanz, R., et alSilent 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., and 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(2), 793-798 (2000).

    5. Kawahara, T.L.A., Michishita, E., Adler, A.S., et alSIRT6 links histone H3 lysine 9 deacetylation to NF- k B-dependent gene expression and organismal life span. Cell 136, 62-74 (2009).

    6. Michishita, E., McCord, R.A., Berber, E., et alSIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin. Nature 452, 492-496 (2008).