SIRT7 (human recombinant)
Cayman Chemical Item Number 10316
SIR2L7; Sirtuin 7; Silent Information Regulator 7; SIR2-like protein 7; NAD-dependent deacetylase 7
SIRT7 (human recombinant)
Description
Source:
Full length (2-400 aa) recombinant N-terminal hexahistidine tagged SIRT7, expressed in E. coli
·
Mr:
49.3 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-SIRT7.4 Recently, SIRT7 has been shown to activate transcription of RNA polymerase I and deacetylate p53.5 SIRT7 prevents progressive functional deterioration of the heart, and is suggested to play an important role in regulation of stress responses and cell death in the heart.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
Lavu, S., Boss, O., Elliot, P.J., et al. Sirtuins-novel therapeutic targets to treat age-associated diseases. Nat Rev Drug Discov 7 841-853 (2008).
6
Vakhrusheva, O., Smolka, C., Gajawada, P., et al. Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice. Circ Res 102 703-710 (2008).
| Synonyms |
- SIR2L7
- Sirtuin 7
- Silent Information Regulator 7
- SIR2-like protein 7
- NAD-dependent deacetylase 7
|
| Formulation |
50 mM sodium phosphate, pH 7.2, containing 100 mM sodium chloride, 5 mM DTT, and 20% glycerol |
| Purity |
≥85% |
| Stability |
6 months |
| Storage |
-80°C |
| Shipping |
Dry ice
in continental US; may vary elsewhere
|
Background Reading
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).
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).
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).
Vakhrusheva, O., Smolka, C., Gajawada, P., et al. Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice. Circ Res 102 703-710 (2008).
Frye, R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 273 793-798 (2000).
Lavu, S., Boss, O., Elliot, P.J., et al. Sirtuins-novel therapeutic targets to treat age-associated diseases. Nat Rev Drug Discov 7 841-853 (2008).
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Pricing updated 2012-02-11.
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