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SIRT3 (human recombinant)

Cayman Chemical Item Number 10011194

Sirtuin 3; Silent Information Regulator 3; NAD-dependent Deacetylase 3; SIR2-like Protein 3; SIR2L3; Mitochondrial Nicotinamide Adenine Dinuclear-dependent Deacetylase

SIRT3 (human recombinant)

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Description

Source: active recombinant N-terminal His-tagged SIRT3 amino acids 101-399 purified from E. coli · Mr: 37 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 (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

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., 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 273 793-798 (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. J Biol Chem 280(14) 13560-13567 (2005).

Synonyms
  • Sirtuin 3
  • Silent Information Regulator 3
  • NAD-dependent Deacetylase 3
  • SIR2-like Protein 3
  • SIR2L3
  • Mitochondrial Nicotinamide Adenine Dinuclear-dependent Deacetylase
Formulation 50 mM sodium phosphate, pH 7.2, containing 100 mM sodium chloride and 20% glycerol
Purity ≥90%
Stability 9 months
Storage -80°C
Shipping Dry ice in continental US; may vary elsewhere

Background Reading

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).

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).

Shi, T., Wang, F., Stieren, E., et al. SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J Biol Chem 280(14) 13560-13567 (2005).

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).

Frye, R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 273 793-798 (2000).

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).

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).

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).

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Size Price Quantity Subtotal
25 µg $98.00 $0.00
50 µg $186.00 $0.00
100 µg $353.00 $0.00
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Pricing updated 2012-05-25. Prices are subject to change without notice.

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Warning This product is not for human or veterinary use.

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