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Useful for inhibitor screening or characterizing enzyme kinetics
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Includes optimal substrate selected from a panel of acetylated sites in p53 and histones
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Supplied with enough recombinant enzyme for 96 assays (1 x 96-well plate)
A FLUOR DE LYS® fluorescent assay system. The SIRT1 Fluorescent Activity Assay/Drug Discovery Kit is a complete assay system designed to measure the lysyl deacetylase activity of the recombinant human SIRT1 included in the kit. The kit is ideal for chemical library screening for candidate inhibitors or activators or kinetic assay of the enzyme under varying conditions. The FLUOR DE LYS® SIRT1 assay is based on the FLUOR DE LYS® SIRT1 Substrate and FLUOR DE LYS® Developer II combination. The assay procedure has two steps. First, the FLUOR DE LYS® SIRT1 Substrate, which contains a peptide comprising amino acids 379-382 of human p53 (Arg-His-Lys-Lys(Ac)). Deacetylation of the substrate sensitizes the substrate so that, in the second step, treatment with the FLUOR DE LYS®Developer II produces a fluorophore.
Figure: Reaction Scheme of the SIRT1 Fluorescent Activity Assay*. NAD+-dependent deacetylation of the substrate by recombinant human SIRT1 sensitizes it to Developer II, which then generates a fluorophore (symbol). The fluorophore is excited with 360 nm light and the emitted light (460 nm) is detected on a fluorometric plate reader. NAD+ is consumed in the reaction to produce nicotinamide (NAM) and O-acetyl-ADP-ribose.
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Product Details
| Alternative Name: | Sirtuin 1 fluorescent assay kit |
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| Applications: | Fluorescent detection, HTS
Activity assay, Cell-based assays
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| Use/Stability: | Store all components except the microplates and instruction booklet at -80°C for the highest stability. The SIRT1 enzyme, (Prod. No. BML-SE239), must be handled with particular care in order to retain maximum enzymatic activity. Defrost it quickly in a RT water bath or by rubbing between fingers, then immediately store on an ice bath. The remaining unused enzyme should be refrozen quickly, by placing at -80°C. If possible, snap freeze in liquid nitrogen or a dry ice/ethanol bath. To minimize the number of freeze/thaw cycles, aliquot into separate tubes and store at -80°C. The 5x Developer II (Prod. No. BML-KI176) can be prone to precipitation if thawed too slowly. It is best to thaw this reagent in a room temperature water bath and, once thawed, transfer immediately onto ice. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Contents: | SIRT1 (Sirtuin 1, hSir2SIRT1) (human, recombinant) (Prod. No. BML-SE239)
(100 U; One U=1 pmol/min at 37°C, 250 µM, FLUOR DE LYS® Substrate (Prod. No. BML-KI104), 500 µM NAD ; Recombinant enzyme dissolved in 25mM TRIS, pH 7.5, 100mM sodium chloride, 5mM dithiothreitol and 10% glycerol. See vial label for activity and protein concentrations
Storage: -80°C; AVOID FREEZE/THAW CYCLES!
FLUOR DE LYS® SIRT1, Deacetylase Substrate (Prod. No. BML-KI177)
(100µl; 5mM solution in 50mM TRIS/Cl, pH 8.0, 137mM sodium chloride, 2.7mM potassium chloride, 1mM magnesium chloride)
Storage: -80°C
FLUOR DE LYS® Developer II Concentrate (5x) (Prod. No. BML-KI176)
(5 x 250 µl; 5x Stock Solution; Dilute in Assay Buffer before use
Storage: -80°C
NAD (Sirtuin Substrate) (Prod. No. BML-KI282)
(500 µl; 50 mM β-Nicotinamide adenine dinucleotide (oxidized form) in 50mM TRIS/CL, pH 8.0, 137mM sodium chloride, 2.7mM potassium chloride, 1mM magnesium chloride)
Storage: -80°C
Nicotinamide (Sirtuin Inhibitor) (Prod. No. BML-KI283)
(500µl; 50 mM Nicotinamide in 50mM TRIS/Cl, pH 8.0, 137mM sodium chloride, 2.7mM potassium chloride, 1mM magnesium chloride)
Storage: -80°C
Resveratrol (Sirtuin Activator) (Prod. No. BML-KI284)
(10 mg; Solid MW: 228.2, soluble in DMSO or 100% ethanol (to 100mM)
Storage: -80°C
Suramin sodium (Sirtuin Inhibitor) (Prod. No. BML-KI285)
(10 mg; Solid MW: 1429.2, soluble in water or assay buffer (to 25mM))
Storage: -80°C
FLUOR DE LYS® Deacetylated Standard (Prod. No. BML-KI142)
(30 µl; 10mM in DMSO)
Storage: -80°C
Sirtuin Assay Buffer
(50mM TRIS/Cl, pH 8.0, 137mM sodium chloride, 2.7mM potassium chloride, 1mM magnesium chloride, 1 mg/ml bovine serum albumin) (Prod. No. BML-KI286) (20 ml)
Storage: -80°C
1/2 volume microplates (Prod. No. 80-2407)
1 clear and 1 white, 96-well
Storage: Room temperature |
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| Scientific Background: | Yeast Sir2 (Silent information regulator 2) is the founding exemplar of the ’sirtuins’, an apparently ancient group of enzymes that occurs in eukaryotes, the archaea and eubacteria. In yeast and C. elegans, added copies of sirtuin genes extend lifespan and Sir2 is required for the lifespan extension conferred by caloric restriction in yeast. There are seven human sirtuins, which have been designated SIRT1-SIRT7. SIRT1, which is located in the nucleus, is the human sirtuin with the greatest homology to Sir2 and has been shown to exert a regulatory effect on p53 by deacetylation of lysine-382. Dr. Konrad Howitz at Enzo Life Sciences carried out a screen for modulators of SIRT1 activity which yielded a number of small molecule activators, all of which were plant polyphenols. Several of these Sirtuin Activating Compounds (STACs) extended yeast lifespan in a way that mimicked caloric restriction. Resveratrol, the most potent of these STACs activated SIRT1 in human cells and enhanced the survival rate of cells stressed by irradiation. |
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| Technical Info/Product Notes: | Cited example:
HTS application. Use of 384-well plates with this kit. |
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| UniProt ID: | Q96EB6 |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Inhibition of phosphodiesterase 5A by tadalafil improves SIRT1 expression and activity in insulin-resistant podocytes: D. Rogacka, et al.; Cell. Signal.
105, 110622 (2023),
Abstract;
Augmentation of NAD+ by Dunnione Ameliorates Imiquimod-Induced Psoriasis-Like Dermatitis in Mice: S.H. Lee, et al. ; J. Inflamm. Res.
15, 4623 (2022),
Abstract;
eNAMPT actions through nucleus accumbens NAD+/SIRT1 link increased adiposity with sociability deficits programmed by peripuberty stress: L. Morató, et al.; Sci. Adv.
8, eabj9109 (2022),
Abstract;
Enhancement of cGMP-dependent pathway activity ameliorates hyperglycemia-induced decrease in SIRT1-AMPK activity in podocytes: Impact on glucose uptake and podocyte function: D. Rogacka, et al.; Biochim. Biophys. Acta Mol. Cell Res.
1869, 119362 (2022),
Abstract;
MHY2245, a Sirtuin Inhibitor, Induces Cell Cycle Arrest and Apoptosis in HCT116 Human Colorectal Cancer Cells: Y.J. Kang, et al.; Int. J. Mol. Sci.
23, 1590 (2022),
Abstract;
Mitochondrial activity is the key to the protective effect of β-Lapachone, a NAD+ booster, in healthy cells against cisplatin cytotoxicity: S.Y. Lin, et al.; Phytomedicine
101, 154094 (2022),
Abstract;
Analysis of Sirtuin 1 and Sirtuin 3 at Enzyme and Protein Levels in Human Breast Milk during the Neonatal Period: K. Hase, et al.; Metabolites
11, 348 (2021),
Abstract;
Full Text
Involvement of nitric oxide synthase/nitric oxide pathway in the regulation of SIRT1-AMPK crosstalk in podocytes: Impact on glucose uptake: D. Rogacka, et al.; Arch. Biochem. Biophys.
709, 108985 (2021),
Abstract;
Perfluorooctane sulfonate continual exposure impairs glucose-stimulated insulin secretion via SIRT1-induced upregulation of UCP2 expression: X. Duan, et al.; Environ. Pollut.
278, 116840 (2021),
Abstract;
Quercetin 3,5,7,3',4'-pentamethyl ether from Kaempferia parviflora directly and effectively activates human SIRT1: M. Zhang, et al.; Commun. Biol.
4, 209 (2021),
Abstract;
Full Text
Silymarin ameliorates the disordered glucose metabolism of mice with diet-induced obesity by activating the hepatic SIRT1 pathway: B. Feng, et al.; Cell. Signal.
84, 110023 (2021),
Abstract;
SIRT1-Dependent Upregulation of BDNF in Human MicrogliaChallenged with Aβ: An Early but Transient Response Rescuedby Melatonin: G.I. Caruso, et al.; Biomedicines
9, 466 (2021),
Abstract;
Structure-Guided Design of a Small-Molecule Activator of Sirtuin-3 that Modulates Autophagy in Triple Negative Breast Cancer: J. Zhang, et al.; J. Med. Chem.
64, 114192 (2021),
Abstract;
Unexpected beta-amyloid production by middle doses of resveratrol through stabilization of APP protein and AMPK-mediated inhibition of trypsin-like proteasome activity i: B.G. Jang, et al.; Food Chem. Toxicol.
152, 112185 (2021),
Abstract;
Isoparvifuran isolated from Dalbergia odorifera attenuates H2O2-induced senescence of BJ cells through SIRT1 activation and AKT/mTOR pathway inhibition: Z. Yin, et al.; Biochem. Biophys. Res. Commun.
533, 925 (2020),
Abstract;
Microorganisms Associated with the Marine Sponge Scopalina hapalia: A Reservoir of Bioactive Molecules to Slow Down the Aging Process: C.S. Hassane, et al.; Microorganisms
20, 1262 (2020),
Application(s): Sirtuin activation by microbial crude extracts.,
Abstract;
Novel SIRT Inhibitor, MHY2256, Induces Cell Cycle Arrest, Apoptosis, and Autophagic Cell Death in HCT116 Human Colorectal Cancer Cells: M.J. Kim, et al.; Biomol. Ther. (Seoul)
28, 561 (2020),
Abstract;
Full Text
Osirisynes G-I, New Long-Chain Highly Oxygenated Polyacetylenes from the Mayotte Marine Sponge Haliclona sp.: P.E. Campos, et al.; Mar. Drugs
18, 350 (2020),
Abstract;
Shrimp SIRT1 activates of the WSSV IE1 promoter independently of the NF-κB binding site: Z.N. Kao, et al.; Fish Shellfish Immunol.
106, 910 (2020),
Application(s): Sirt1 activity in shrimp hempcyte samples,
Abstract;
A novel form of Deleted in breast cancer 1 (DBC1) lacking the N-terminal domain does not bind SIRT1 and is dynamically regulated in vivo: L. Santos, et al.; Sci. Rep.
9, 14381 (2019),
Abstract;
Full Text
Antiproliferative activity of (R)-4'-methylklavuzon on hepatocellular carcinoma cells and EpCAM+/CD133+ cancer stem cells via SIRT1 and Exportin-1 (CRM1) inhibition: M. Delman, et al.; Eur. J. Med. Chem.
180, 224 (2019),
Abstract;
Molecular and Cellular Characterization of SIRT1 Allosteric Activators: M.B. Schultz, et al.; Methods Mol. Biol.
1983, 133 (2019),
Abstract;
Pharmacophore modeling and virtual screening studies to identify novel selective SIRT2 inhibitors: G. Eren, et al.; J. Mol. Graph. Model.
10, 1313 (2019),
Abstract;
Regulation of sirtuin expression in autoimmune neuroinflammation: Induction of SIRT1 in oligodendrocyte progenitor cells: T. Prozorovski, et al.; Neurosci. Lett.
704, 116 (2019),
Abstract;
Decrease in membrane phospholipids unsaturation correlates with myocardial diastolic dysfunction: T. Yamamoto, et al.; PLoS One
13, e30533011 (2018),
Abstract;
Erythropoietin alleviates hepatic steatosis by activating SIRT1-mediated autophagy: T. Hong, et al.; Biochim. Biophys. Acta Mol. Cell. Biol. Lipids
1863, 595 (2018),
Abstract;
Honokiol Ameliorates Myocardial Ischemia/Reperfusion Injury in Type 1 Diabetic Rats by Reducing Oxidative Stress and Apoptosis through Activating the SIRT1-Nrf2 Signaling Pathway: B. Zhang, et al.; Oxid. Med. Cell. Longev.
2018, 3159801 (2018),
Abstract;
Full Text
Resveratrol ameliorates prenatal progestin exposure-induced autism-like behavior through ERβ activation: W. Xie, et al.; Mol. Autism
9, 43 (2018),
Abstract;
Full Text
SIRT1 activator E1231 protects from experimental atherosclerosis and lowers plasma cholesterol and triglycerides by enhancing ABCA1 expression: T. Feng, et al.; Atherosclerosis
274, 172 (2018),
Abstract;
Two Novel Proline-Containing Catechin Glucoside from Water-Soluble Extract of Codonopsis pilosula: F.Y. Qin, et al.; Molecules
23, E180 (2018),
Application(s):SIRT1 Inhibition,
Abstract;
Full Text
A novel SIRT1 inhibitor, 4bb induces apoptosis in HCT116 human colon carcinoma cells partially by activating p53: A. Ghosh, et al.; Biochem. Biophys. Res. Commun.
488, 562 (2017),
Abstract;
Aquatide Activation of SIRT1 Reduces Cellular Senescence through a SIRT1-FOXO1-Autophagy Axis: C.J. Lim, et al.; Biomol. Ther.
25, 511 (2017),
Abstract;
Full Text
Design, synthesis of allosteric peptide activator for human SIRT1 and its biological evaluation in cellular model of Alzheimer's disease: R. Kumar, et al.; Eur. J. Med. Chem.
127, 909 (2017),
Abstract;
Glutaredoxin-1 Deficiency Causes Fatty Liver and Dyslipidemia by Inhibiting Sirtuin-1: D. Shao, et al.; Antioxid. Redox Signal.
27, 313 (2017),
Abstract;
Full Text
Obesity-Linked Phosphorylation of SIRT1 by Casein Kinase 2 Inhibits Its Nuclear Localization and Promotes Fatty Liver: S.E. Choi, et al.; Mol. Cell. Biol.
37, e00006 (2017),
Abstract;
Full Text
Phosphorylated SIRT1 associates with replication origins to prevent excess replication initiation and preserve genomic stability: K. Utani, et al.; Nucleic Acids Res.
45, 7807 (2017),
Abstract;
Full Text
Scopolin ameliorates high-fat diet induced hepatic steatosis in mice: potential involvement of SIRT1-mediated signaling cascades in the liver: A. Yoo, et al.; Sci. Rep.
7, 2251 (2017),
Abstract;
Full Text
Serum CCL20 and its association with SIRT1 activity in multiple sclerosis patients: R. Li, et al.; J. Neuroimmunol.
313, 56 (2017),
Abstract;
SIRT1 may play a crucial role in overload-induced hypertrophy of skeletal muscle: E. Koltai, et al.; J. Physiol.
595, 3361 (2017),
Abstract;
Full Text
Caspase-2 deficiency accelerates chemically induced liver cancer in mice: S. Shalini, et al.; Cell Death Differ.
23, 1727 (2016),
Application(s): Measurement of liver metabolites and Sirt1 and Sirt3 activities,
Abstract;
Conditioned Medium from Early-Outgrowth Bone Marrow Cells Is Retinal Protective in Experimental Model of Diabetes: D.A. Duarte, et al.; PLoS One
11, e0147978 (2016),
Application(s): Measured SIRT1 activity,
Abstract;
Full Text
Dunnione ameliorates cisplatin ototoxicity through modulation of NAD+ metabolism: H.J. Kim, et al.; Hear Res.
333, 235 (2016),
Application(s): SIRT1 activity Assay,
Abstract;
Hormetic shifting of redox environment by pro-oxidative resveratrol protects cells against stress: A. Plauth, et al.; Free Radic. Biol. Med.
99, 608 (2016),
Abstract;
How much successful are the medicinal chemists in modulation of SIRT1: A critical review: A. Kumar, et al.; Eur. J. Med. Chem.
119, 45 (2016),
Abstract;
Protective Effects of Hydrogen Sulfide in the Ageing Kidney: C.L. Hou, et al.; Oxid. Med. Cell. Longevity
2016, 7570489 (2016),
Abstract;
Full Text
SIRT1-Activating Compounds (STAC) Negatively Regulate Pancreatic Cancer Cell Growth and Viability Through a SIRT1 Lysosomal-Dependent Pathway: C.C. Chini et al.; Clin. Cancer Res.
22, 2496 (2016),
Abstract;
SIRT1-AMPK crosstalk is involved in high glucose-dependent impairment of insulin responsiveness in primary rat podocytes: D. Rogacka, et al.; Exp. Cell. Res.
349, 328 (2016),
Abstract;
SIRT3 Deacetylates Ceramide Synthases: Implications for Mitochondrial Dysfunction and Brain Injury: S.A. Novgorodov, et al.; J. Biol. Chem.
291, 1957 (2016),
Application(s): Deacetylation assay with mouse brain cells,
Abstract;
Full Text
The peroxisome proliferator-activated receptor γ agonist pioglitazone prevents NF-κB activation in cisplatin nephrotoxicity through the reduction of p65 acetylation via the AMPK-SIRT1/p300 pathway: J. Zhang, et al.; Biochem. Pharmacol.
101, 100 (2016),
Application(s): SIRT1 deacetylase activity,
Abstract;
BET Inhibition Upregulates SIRT1 and Alleviates Inflammatory Responses: T. Kokkola, et al.; Chembiochem
16, 1997 (2015),
Abstract;
Full Text
Curcumin as therapeutics for the treatment of head and neck squamous cell carcinoma by activating SIRT1: A. Hu, et al.; Sci. Rep.
5, Article number 13429 (2015),
Application(s): Deacetylase assay in HNSCC cell lines,
Abstract;
Full Text
Discovery of bicyclic pyrazoles as class III histone deacetylase SIRT1 and SIRT2 inhibitors: E. Therrien, et al.; Bioorg. Med. Chem. Lett.
25, 2514 (2015),
Abstract;
Dunnione ameliorates cisplatin-induced small intestinal damage by modulating NAD+ metabolism: A. Pandit, et al.; Biochem. Biophys. Res. Commun.
467, 697 (2015),
Application(s): Determination of SIRT1 activity,
Abstract;
Leucine Amplifies the Effects of Metformin on Insulin Sensitivity and Glycemic Control in Diet-Induced Obese Mice: L. Fu, et al.; Metabolism
64, 845 (2015),
Application(s): Assay,
Abstract;
SIRT1 inhibition in pancreatic cancer models: Contrasting effects in vitro and in vivo: C. E. Oon, et al.; Eur. J. Pharmacol.
757, 59 (2015),
Application(s): Fluorescence microscopy ,
Abstract;
SIRT5 regulation of ammonia-induced autophagy and mitophagy: L. Polletta, et al.; Autophagy
11, 253 (2015),
Abstract;
Full Text
Virtual screening approach of sirtuin inhibitors results in two new scaffolds: P. Kokkonen, et al.; Eur. J. Pharm. Sci.
76, 27 (2015),
Application(s): Assay,
Abstract;
A redox-resistant sirtuin-1 mutant protects against hepatic metabolic and oxidant stress: D. Shao, et al.; J. Biol. Chem.
289, 7293 (2014),
Abstract;
Coumestrol induces mitochondrial biogenesis by activating Sirt1 in cultured skeletal muscle cells: D.B. Seo, et al.; J. Agric. Food Chem.
62, 4298 (2014),
Abstract;
Design, synthesis, and biological activity of NCC149 derivatives as histone deacetylase 8-selective inhibitors: T. Suzuki, et al.; ChemMedChem.
9, 657 (2014),
Abstract;
Modulation of the AMPK/Sirt1 axis during neuronal infection by herpes simplex virus type 1: C. Martin, et al.; J. Alzheimers Dis.
42, 301 (2014),
Abstract;
Resveratrol delays Wallerian degeneration in a NAD(+) and DBC1 dependent manner: A. Calliari, et al.; Exp. Neurol.
251, 91 (2014),
Abstract;
Sirtuin 1 activity in peripheral blood mononuclear cells of patients with osteoporosis: M. Godfrin-Valnet, et al.; Med. Sci. Monit. Basic Res.
20, 142 (2014),
Abstract;
Full Text
Synergistic Effects of Polyphenols and Methylxanthines with Leucine on AMPK/Sirtuin-Mediated Metabolism in Muscle Cells and Adipocytes: A. Bruckbauer & M.B. Zemel; PLoS One
9, e89166 (2014),
Abstract;
Full Text
Tissue-specific deregulation of selected HDACs characterizes ALS progression in mouse models: pharmacological characterization of SIRT1 and SIRT2 pathways: C. Valle, et al.; Cell Death Dis.
5, e1296 (2014),
Abstract;
Full Text
Cytotoxicity and cell death mechanisms induced by a novel bisnaphthalimidopropyl derivative against the NCI-H460 non-small lung cancer cell line: R.T. Lima, et al.; Anticancer Agents Med. Chem.
13, 414 (2013),
Abstract;
Dietary resveratrol prevents development of high-grade prostatic intraepithelial neoplastic lesions: involvement of SIRT1/S6K axis: G. Li, et al.; Cancer Prev. Res. (Phila)
6, 27 (2013),
Abstract;
Full Text
Effects of Resveratrol on the Recovery of Muscle Mass Following Disuse in the Plantaris Muscle of Aged Rats: B. Bennett, et al.; PLoS One
8, e83518 (2013),
Abstract;
Full Text
Modulation of p53 C-terminal acetylation by mdm2, p14ARF, and cytoplasmic SirT2: I.M. van Leeuwen, et al.; Mol. Cancer Ther.
12, 471 (2013),
Abstract;
Full Text
Rejuvenating sirtuins: the rise of a new family of cancer drug targets: S. Bruzzone, et al.; Curr. Pharm. Des.
19, 614 (2013),
Abstract;
Full Text
Resveratrol administration or SIRT1 overexpression does not increase LXR signaling and macrophage-to-feces reverse cholesterol transport in vivo: J.C. Escola-Gil, et al.; Transl. Res.
161, 110 (2013),
Abstract;
Synergistic effects of metformin, resveratrol, and hydroxymethylbutyrate on insulin sensitivity: A. Bruckbauer & M.B. Zemel; Diabetes Metab. Syndr. Obes.
6, 93 (2013),
Abstract;
Full Text
Tenovin-D3, a novel small-molecule inhibitor of sirtuin SirT2, increases p21 (CDKN1A) expression in a p53-independent manner: A.R. McCarthy, et al.; Mol. Cancer Ther.
12, 352 (2013),
Abstract;
Full Text
A maternal high-fat diet modulates fetal SIRT1 histone and protein deacetylase activity in nonhuman primates: M.A. Suter, et al.; FASEB J.
26, 5106 (2012),
Application(s): HDAC activity in fetal macaque liver or Cos-1 cell extracts,
Abstract;
Full Text
Role of deleted in breast cancer 1 (DBC1) protein in SIRT1 deacetylase activation induced by protein kinase A and AMP-activated protein kinase: V. Nin, et al.; J. Biol. Chem.
287, 23489 (2012),
Application(s): SIRT1 activity measurement in cells,
Abstract;
Full Text
SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity: M. Pan, et al.; J. Biol. Chem.
287, 2468 (2012),
Abstract;
Full Text
Synergistic effects of leucine and resveratrol on insulin sensitivity and fat metabolism in adipocytes and mice: A. Bruckbauer, et al.; Nutr. Metab. (Lond.)
9, 77 (2012),
Abstract;
Full Text
Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila: C. Burnett, et al.; Nature
477, 482 (2011),
Application(s): Drosophila's Sir2 deacetylation assay,
Abstract;
Full Text
Effects of dairy consumption on SIRT1 and mitochondrial biogenesis in adipocytes and muscle cells: A. Bruckbauer & M.B. Zemel; Nutr. Metab. (Lond.)
8, 91 (2011),
Abstract;
Full Text
Fatty liver is associated with reduced SIRT3 activity and mitochondrial protein hyperacetylation: A.A. Kendrick, et al.; Biochem. J.
433, 505 (2011),
Application(s): SIRT1 activity in mouse liver cells,
Abstract;
Full Text
SIRT1 Activates MAO-A in the Brain to Mediate Anxiety and Exploratory Drive: S. Libert, et al.; Cell
147, 1459 (2011),
Abstract;
Full Text
SIRT1 activation by resveratrol ameliorates cisplatin-induced renal injury through deacetylation of p53: D.H. Kim, et al.; Am. J. Physiol. Renal Physiol.
301, F427 (2011),
Application(s): Activity of immunoprecipitated SIRT1,
Abstract;
Full Text
SIRT inhibitors induce cell death and p53 acetylation through targeting both SIRT1 and SIRT2: B. Peck, et al.; Mol. Cancer Ther.
9, 844 (2010),
Abstract;
Full Text
SIRT1-independent mechanisms of the putative sirtuin enzyme activators SRT1720 and SRT2183: J.L. Huber, et al.; Future Med. Chem.
2, 1751 (2010),
Abstract;
Identification and characterization of novel sirtuin inhibitor scaffolds: B.D. Sanders, et al.; Bioorg. Med. Chem.
17, 7031 (2009),
Application(s): HTS application. Use of 384-well plates with this kit,
Abstract;
Full Text
General Literature References
Calorie restriction in rhesus monkeys: J.A. Mattison; Exp. Gerontol.
38, 35 (2003),
Abstract;
Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae: R. M. Anderson et al.; Nature
423, 181 (2003),
Abstract;
Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan: K. T. Howitz et al.; Nature
425, 191 (2003),
Abstract;
Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence: E. Langley et al.; Embo J.
21, 2383 (2002),
Abstract;
Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1: K.J. Bitterman et al.; J. Biol. Chem.
277, 45099 (2002),
Abstract;
hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase: H. Vaziri et al.; Cell
107, 149 (2001),
Abstract;
Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans: H. A. Tissenbaum et al.; Nature
410, 227 (2001),
Abstract;
Negative control of p53 by Sir2alpha promotes cell survival under stress: J. Luo et al.; Cell
107, 137 (2001),
Abstract;
A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family: J. S. Smith et al.; PNAS
97, 6658 (2000),
Abstract;
Caloric restriction and aging: an update: E.J. Masoro et al.; Exp. Gerontol.
35, 299 (2000),
Abstract;
Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product: J. C. Tanny et al.; PNAS
98, 415 (2000),
Abstract;
Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins: R. A. Frye et al.; Biochem. Biophys. Res. Commun.
273, 793 (2000),
Abstract;
Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae: S.J. Lin et al.; Science
289, 2126 (2000),
Abstract;
Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose: K. G. Tanner et al.; PNAS
97, 14178 (2000),
Abstract;
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase: S. Imai et al.; Nature 403, 795 (2000),
The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms: M. Kaeberlein et al.; Genes Dev.
13, 2570 (1999),
Abstract;
Silencers, silencing, and heritable transcriptional states: P. Laurenson et al.; Microbiol Rev
56, 543 (1992),
Abstract;
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