SIRT2 (human recombinant)
Cayman Chemical Item Number 10011191
Silent Information Regulator 2; Sirtuin 2; SIR2-like Protein 2; NAD-dependent Deacetylase 2; SIR2L2
Description
Source:
active recombinant N-terminal His-tagged SIRT2 amino acids 2-389, purified from E.coli
·
Mr:
44.2 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, 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 hyperpolid 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
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
Dali-Youcef, N., Lagouge, M., Froelich, S., et al. Sirtuins: The 'magnificent seven', function, metabolism and longevity. Ann Med 39 335-345 (2007).
6
Tang, B.L., and Chua, C.E.L. SIRT2, tubulin deacetylation, and oligodendroglia differentiation. Cell Motil Cytoskeleton 65 179-182 (2008).
| Synonyms |
- Silent Information Regulator 2
- Sirtuin 2
- SIR2-like Protein 2
- NAD-dependent Deacetylase 2
- SIR2L2
|
| 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
Tang, B.L., and Chua, C.E.L. SIRT2, tubulin deacetylation, and oligodendroglia differentiation. Cell Motil Cytoskeleton 65 179-182 (2008).
Dali-Youcef, N., Lagouge, M., Froelich, S., et al. Sirtuins: The 'magnificent seven', function, metabolism and longevity. Ann Med 39 335-345 (2007).
Frye, R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 273 793-798 (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).
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).
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Pricing updated 2012-05-25.
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