10011194  SIRT3 (human recombinant)

Sirtuin 3; Silent Information Regulator 2; SIR2

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• See more Colorimetric Assay; Enzyme Activity; Fluorescence; High Throughput Screening; Inhibitor Screening Assay; Western Blot; Enzymes; Histone Deacetylase; Proteins; Recombinant Proteins; Chromatin Research; Drug Discovery; Epigenetics; Histone Modification; Metabolism

For active pharmaceutical ingredients (APIs) related to SIRT3 (human recombinant), see Cayman Pharma

Source: recombinant N-terminal Hexahistidine-tagged SIRT3 amino acids 101-399 purified from E. coli · Mr: 37.0 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., 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., 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).

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Pricing Information

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Size Price Quantity
25 µg €115.00
50 µg €218.00
100 µg €411.00
Pricing updated 2010-03-12.
Prices are subject to change without notice.