Active, purified human recombinant enzyme
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SIRT1 (human, recombinant)

Item No. 10011190

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • NAD-dependent Deacetylase 1
  • Silent Information Regulator 2
  • SIR2L1
  • SIR2-like Protein 1
  • Sirtuin 1
Purity
≥70% estimated by SDS-PAGE
Source
Recombinant N-terminal GST-tagged protein expressed in E. coli
Amino Acids
193-747
MW
89.2 kDa
Formulation (Request formulation change)
50 mM sodium phosphate, pH 7.2, with 100 mM sodium chloride and 20% glycerol
UniProt Accession №
Q96EB6
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

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    100 units

    $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 SIRT1, which is located in the nucleus, is the human sirtuin with the greatest homology to yeast Sir2 (Silent information regulator 2), regulates the activity of the tumor suppressor p53 and inhibist apoptosis.5,6,7

    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. Luo, J., Nikolaev, A.Y., Imai, S.I., 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).