Active, pure human recombinant enzyme
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SIRT2 (human, recombinant)

Item No. 10011191

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • NAD-dependent Deacetylase 2
  • Silent Information Regulator 2
  • SIR2L2
  • SIR2-like Protein 2
  • Sirtuin 2
Purity
≥80% estimated by SDS-PAGE
Source
Active recombinant N-terminal hexahistidine-tagged enzyme amino acids 2-389, expressed in E. coli
MW
43.9 kDa
Formulation (Request formulation change)
50 mM Tris, pH 8.0, with 100 mM sodium chloride and 20% glycerol
UniProt Accession №
Q8IXJ6
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $528

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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 SIRT2 is a cytoplasmic protein responsible for the deacetylation of histone H4 and a-tubulin, a modification important for controlling the cell cycle. Specifically, SIRT2 co-localizes with HDAC6 and microtubules and functions as a mitotic checkpoint in preventing chromosomal instability that can lead to hyperploid cells. SIRT2 is found in many tissues, but is specifically enriched in skeletal muscle, the heart, and in oligodendroglia cells in the brain.5,6

    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 al. Transcriptional 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 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., 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. Dali-Youcef, N., Lagouge, M., Froelich, S., et al. Sirtuins: The 'magnificent seven', function, metabolism and longevity. Ann. Med. 39(5), 335-345 (2007).

    6. Tang, B.L., and Chua, C.E.L. SIRT2, tubulin deacetylation, and oligodendroglia differentiation. Cell Motil. Cytoskeleton 65(3), 179-182 (2008).