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.
Pack Size | Availability | Price/USD | Quantity |
---|---|---|---|
100 μg | 5 days | $ 600.00 |
Description | 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. |
Species | Human |
Expression System | E. coli |
Tag | His |
Accession Number | A0A024QZQ1 |
Synonyms | SIR2L1, sirtuin 1 |
Construction | A DNA sequence encoding the human SIRT1 (Met 193-Ser 747) was expressed with a polyhistide tag at the N-terminus. |
Protein Purity | > 65 % as determined by SDS-PAGE |
Molecular Weight | 62.8 kDa (predicted) |
Endotoxin | Please contact us for more information. |
Formulation | Lyophilized from sterile PBS, pH 7.4, 10% glycerol. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA. |
Reconstitution | A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information. |
Stability & Storage |
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
Shipping |
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. |
Research 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. |
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SIRT1 Protein, Human, Recombinant (His) SIR2L1 sirtuin 1 recombinant recombinant-proteins proteins protein