Active, pure human recombinant enzyme
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SIRT3 (human, recombinant)

Item No. 10011194

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • Mitochondrial Nicotinamide Adenine Dinuclear-dependent Deacetylase
  • NAD-dependent Deacetylase 3
  • Silent Information Regulator 3
  • SIR2L3
  • SIR2-like Protein 3
  • Sirtuin 3
Purity
≥60% estimated by SDS-PAGE
Source
Active recombinant N-terminal His-tagged enzyme amino acids 101-399 purified from E. coli
Amino Acids
101-399
MW
37 kDa (theoretical); 33.5 kDa (observed). The identity of SIRT3 protein was confirmed by mass spectrometry.
Formulation (Request formulation change)
50 mM sodium phosphate, pH 7.2, with 100 mM sodium chloride and 20% glycerol
UniProt Accession №
Q9NTG7
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 (SIRTs) 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 SIRTs, which have been designated SIRT 1-7.4 SIRT3, is a mitochondrial protein, with its N-terminal 25 amino acid residues responsible for its localization.5,6 Synthesized as an enzymatically inactive protein, human SIRT3 is activated by a matrix-processing peptidase.6 Recently, it was demonstrated that SIRT3 is translocated to the mitochondria from the nucleus during cellular stress or by the overexpression of SIRT3 itself.7 In mice, caloric restriction up-regulates SIRT3 expression levels in white and brown adipose tissue (WAT & BAT). Cold exposure also induces SIRT3 in brown adipose tissue (BAT).8 The constitutive expression of SIRT3 promotes the expression of PGC-1a, UCP1, and other genes involved in mitochondrial functions, indicating that SIRT3 modulates adaptive thermogenesis in BAT.8

    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. Onyango, P., Celic, I., McCaffery, J.M., et al. SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria. Proc. Natl. Acad. Sci. USA 99(21), 13653-13658 (2002).

    6. Schwer, B., North, B.J., Frye, R.A., et al. The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J. Cell Biol. 158(4), 647-657 (2002).

    7. Scher, M.B., Vaquero, A., and Reinberg, D. SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev. 21, 920-928 (2007).

    8. Shi, T., Wang, F., Stieren, E., et al. SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. The Journal of Biological Chemisty 280(14), 13560-13567 (2005).