SIRT1 is the closest human homolog of yeast Sir2 (Silent information regulator 2), the founding exemplar of the ”sirtuins” or class III (NAD+-dependent) histone deacetylases (HDACs). The wide array of in vivo targets for SIRT1 deacetylation includes other proteins involved in regulatory post-translational modifications, several histone sites (H4K16, H3K9/K14, H1K26), multiple transcription factors (e.g. p53, NF-kB, FOXOs, PGC-1a) and key metabolic enzymes. SIRT1 has regulatory roles in gene expression and gene silencing, in cellular stress responses (e.g to DNA damage, oxidation and heat), in autophagy, in apoptosis and cell survival and in the circadian clock. SIRT1 activity is upregulated in response to calorie restriction (CR), in part by increased expression, in part by the elevation of cellular NAD+, and is required for downstream CR effects. Given the benefits of CR for the diseases of aging (and possibly longevity per se), the discovery of natural (e.g. resveratrol) and synthetic small molecule SIRT1 activators opened a promising avenue for therapeutic interventions in, for example, type 2 diabetes and neurodegeneration. While the question of whether these compounds act by directly stimulating SIRT1 catalytic activity has been controversial for some years, recent results indicate that this is most likely in fact the case and that activators bind an allosteric site on SIRT1.
ACCESSION #: NM_012238
INCLUDES AMINO ACIDS: 1-747 (C-term.)
TAG(S): N-terminal His-tag
MW: 83.2 kDa
EXPRESSION SYSTEM: E. coli
SUPPLIED AS: Solution of purified recombinant protein in 50 mM Tris/HCl pH 7.5, 100 mM NaCl, 10% glycerol (v/v).
STORAGE: -80°C, aliquot and snap-freeze after first use.
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