SIRT1 Proteins, Antibodies, cDNA Clones Research Reagents

SIRT1 (Sirtuin 1) is a protein coding gene located on human chromosome 10q21.3. SIRT1 is also known as SIR2, SIR2L1 and SIR2alpha. The human SIRT1 gene encodes an 81681 Da protein containing 747 amino acids. The SIRT1 protein is ubiquitously expressed in adrenal, testis and other tissues. Among its related pathways are Simplified Interaction Map Between LOXL4 and Oxidative Stress Pathway and E2F transcription factor network. SIRT1 is related to identical protein binding and transcription factor binding. SIRT2 is an important paralog of SIRT1 gene. SIRT1 is associated with some diseases, including Periapical Periodontitis and Aging.

SIRT1 Protein (1)

    SIRT1 Antibody (7)

      SIRT1 cDNA Clone (1)


      In expression vector

      SIRT1 Background

      SIRT1 belongs to the sirtuin family. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. SIRT1 is included in class I of the sirtuin family. It is a NAD-dependent protein deacetylase, which regulates processes such as apoptosis and muscle differentiation by deacetylating key proteins. It deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce proapoptotic program and modulate cell senescence. SIRT1 also deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. It is involved in HES1- and HEY2-mediated transcriptional repression. SIRT1 inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. It may serve as a sensor of the cytosolic ratio of NAD(+)/NADH, which is essential in skeletal muscle cell differentiation. It also deacetylates 'Lys-16' of histone H4 (in vitro). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus.

      SIRT1 References

      • Sharma A, et al. (2012) Interactomic and pharmacological insights on human Sirt-1. Front Pharmacol. 3-40.
      • Sun C, et al. (2007) SIRT1 improves insulin sensitivity under insulin-resistant conditions by repressing PTP1B. Cell Metab. 6(4):307-19.
      • Rodgers JT, et al. (2005) Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature. 434(7029):113-8.
      • Nemoto S, et al. (2005) SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1{alpha}. J Biol Chem. 280(16):16456-60.

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