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Sirtuin

Custom & Catalog Recombinant Proteins

Histone deacetylases (HDACs) act as transcriptional repressors of genes catalyzing the removal of acetyl groups from a å-N-acetyl lysine of histone.1

Sirtuin 1 (SIRT1), the human homolog of yeast Sir2 (Silent Information Regulator 2), is the most studied of the seven members of sirtuin family. SIRT1 have been implicated in several important cellular processes, including genomic stability and DNA repair,2,.3 p53-mediated apoptosis,4 adipogenesis,5 and aging.6,7

Sirtuin 2 (SIRT2) belongs to a unique class of nicotinamide adenine dinucleotide (NAD+)-dependent deacetylases (class III HDACs) that target multiple protein substrates to execute diverse biological functions.

DescriptionSize Reference USD Qty  
Human Sirtuin 1, recombinant - 10 µg10 µg AS-72212 98.00Add to cart
Human Sirtuin 2, recombinant - 10 µg10 µg AS-72187 98.00Add to cart


Size:

  10 µg

Storage:

  Store at -80°C. Avoid multiple freeze/thaw cycles.

Histone deacetylases (HDACs) act as transcriptional repressors of genes catalyzing the removal of acetyl groups from a å-N-acetyl lysine of histone.1

Sirtuin 1 (SIRT1), the human homolog of yeast Sir2 (Silent Information Regulator 2), is the most studied of the seven members of sirtuin family. SIRT1 have been implicated in several important cellular processes, including genomic stability and DNA repair,2,.3 p53-mediated apoptosis,4 adipogenesis,5 and aging.6,7

Sirtuin 2 (SIRT2) belongs to a unique class of nicotinamide adenine dinucleotide (NAD+)-dependent deacetylases (class III HDACs) that target multiple protein substrates to execute diverse biological functions.

The recombinant human Sirtuin 1 (GenBank Accession #: NM_012238) with 193- 741 amino acids and GST tag at its N-terminal was expressed in E. coli. The molecular mass of the enzyme is approximately 87.2 kDa on SDS-PAGE.

The recombinant human Sirtuin 2 (GenBank Accession #: NM_030593) with 13-319 amino acids and His tag at its C-terminal was expressed in E. coli. The molecular mass of the enzyme is approximately 35.5 kDa on SDS-PAGE.


References:


  1. Sterner, DE. et al. Microbiol. Mol. Biol. Rev. 64, 435 (2000).
  2. Yamagata, K and Kitabayashi, I. Biochem Biophys Res Commun. 390, 1355 (2009).
  3. Wang, RH. et al. Cancer Cell. 14, 312 (2008).
  4. Vaziri, H. et al. Cell. 107, 149 (2001).
  5. Picard, F. et al. Nature. 429, 771 (2004).
  6. Cohen, HY. et al. Science 305, 390 (2004).
  7. Trapp, J. and Jung, M. Curr. Drug Target 7, 1553 (2006).

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