SIRT1 (193-747 aa) (GST-tagged), Human recombinant protein
NAD-dependent Deacetylase 1, SIR2L1, SIR2-like Protein 1, Sirtuin 1, Silent Information Regulator 2
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q96EB6 |
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Calculated MW | 82.9 kDa |
Gene ID | 23411 |
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Gene Symbol | SIRT1 |
Other Names | NAD-dependent Deacetylase 1, SIR2L1, SIR2-like Protein 1, Sirtuin 1, Silent Information Regulator 2 |
Gene Source | Human |
Source | E. coli |
Assay&Purity | SDS-PAGE; ≥60% |
Assay2&Purity2 | N/A; |
Recombinant | Yes |
Results | ≥ 550 pmol/min/mg |
Target/Specificity | SIRT1 |
Format | Liquid |
Storage | -80°C; Supplied as a solution in 50 mM sodium phosphate, pH 7.2, containing 100 mM sodium chloride and 20% glycerol |
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Background
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. There are seven human sirtuins, which have been designated SIRT1-7. SIRT1, which is located in the nucleus, is the human sirtuin with the greatest homology to yeast Sir2 (Silent information regulator 2) and has been shown to regulate the activity of the p53 tumor suppressor and inhibit apoptosis. These results have significant implications regarding an important role of SIRT1 in modulating the sensitivity of cells in the p53-dependent apoptotic response and the possible effect in cancer therapy. Since the growth suppressive function of p53 is strongly enhanced by DNA damaging reagents, it is expected that inhibitors of SIRT1 may be effective anti-cancer drugs.
References
Frye R.A.,et al.Biochem. Biophys. Res. Commun. 260:273-279(1999).
Takata T.,et al.Biochem. Biophys. Res. Commun. 301:250-257(2003).
Deloukas P.,et al.Nature 429:375-381(2004).
Vaziri H.,et al.Cell 107:149-159(2001).
Langley E.,et al.EMBO J. 21:2383-2396(2002).
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