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Join us! · InformexUSA 2012 · New Orleans, Louisiana · February 14-17, 2012 · Booth 2514

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)

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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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Size Price Quantity Subtotal
25 µg $98.00 $0.00
50 µg $186.00 $0.00
100 µg $353.00 $0.00
Bulk Contact
Cart Total $0.00

This product is available in custom sizes and/or larger quantities.

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Pricing updated 2012-02-11. Prices are subject to change without notice.

To ask for assistance with one of our products please contact a Technical Support Scientist.

Warning This product is not for human or veterinary use.

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