SIRT1 recombinant protein

SIRT1 Protein, Human, Recombinant (His Tag)

Cat. Num. AAA8120962

• Gene Names: SIRT1; SIR2L1
• Purity: >65% as determined by SDS-PAGE
• Synonyms: SIRT1; SIRT1 Protein; Human; Recombinant (His Tag); Human SIRT1/SIR2L1 Protein (His Tag); SIR2L1 Protein; sirtuin 1; SIRT1 recombinant protein

• Host: E Coli
• Purity/Purification: >65% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH7.4, 10% glycerol. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
• Sequence: Met193-Ser747

• Species: Human
• Predicted N Terminal: Met
• Tag: N-His
• Protein Construction: A DNA sequence encoding the human SIRT1 (Met 193-Ser 747) was expressed with a polyhistide tag at the N-terminus.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.; 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.

SDS-Page

Related Product Information for SIRT1 recombinant protein

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.

Product Categories/Family for SIRT1 recombinant protein

p53 Pathway

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.

NCBI and Uniprot Product Information

• NCBI GI #: 7657575
• NCBI GeneID: 23411
• NCBI Accession #: NP_036370.2
• NCBI GenBank Nucleotide #: NM_012238.4
• UniProt Accession #: Q96EB6; Q2XNF6; Q5JVQ0; Q9GZR9; Q9Y6F0
• Molecular Weight: 61,066 Da
• NCBI Official Full Name: NAD-dependent protein deacetylase sirtuin-1 isoform a
• NCBI Official Synonym Full Names: sirtuin 1
• NCBI Official Symbol: SIRT1
• NCBI Official Synonym Symbols: SIR2L1
• NCBI Protein Information: NAD-dependent protein deacetylase sirtuin-1; hSIR2; hSIRT1; SIR2alpha; sir2-like 1; sirtuin type 1; SIR2-like protein 1; regulatory protein SIR2 homolog 1; NAD-dependent deacetylase sirtuin-1
• UniProt Protein Name: NAD-dependent protein deacetylase sirtuin-1
• Protein Family: NAD-dependent protein deacetylase sirtuin
• UniProt Gene Name: SIRT1
• UniProt Synonym Gene Names: SIR2L1; hSIRT1; hSIR2; 75SirT1
• UniProt Entry Name: SIR1_HUMAN

NCBI Description

This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2008]

Uniprot Description

SIRT1: an NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separate cellular functions such as cell cycle, response to DNA damage, metobolism, apoptosis and autophagy. Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively. Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction. Essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT). 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. Elevation of NAD(+)/NADP(+) ratio activates SIRT1. Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression. Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG. Involved in liver and muscle metabolism. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and ATG8. Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation. Widely expressed. Inhibited by nicotinamide. Belongs to the sirtuin family. Class I subfamily. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Deacetylase; Apoptosis; EC 3.5.1.-; Nuclear receptor co-regulator

Chromosomal Location of Human Ortholog: 10q21.3

Cellular Component: nucleoplasm; chromatin silencing complex; PML body; mitochondrion; ESC/E(Z) complex; nuclear chromatin; cytoplasm; nucleolus; nuclear inner membrane; nuclear envelope; nuclear heterochromatin; nucleus

Molecular Function: deacetylase activity; protein C-terminus binding; identical protein binding; histone binding; p53 binding; metal ion binding; protein deacetylase activity; transcription factor binding; protein binding; NAD-dependent histone deacetylase activity (H3-K9 specific); enzyme binding; NAD-dependent histone deacetylase activity; bHLH transcription factor binding; mitogen-activated protein kinase binding; histone deacetylase activity; transcription corepressor activity; HLH domain binding; NAD+ ADP-ribosyltransferase activity

Biological Process: establishment and/or maintenance of chromatin architecture; muscle development; viral reproduction; positive regulation of apoptosis; regulation of mitotic cell cycle; positive regulation of caspase activity; protein ubiquitination; negative regulation of prostaglandin biosynthetic process; negative regulation of DNA damage response, signal transduction by p53 class mediator; negative regulation of gene expression, epigenetic; behavioral response to starvation; positive regulation of adaptive immune response; positive regulation of histone H3-K9 methylation; positive regulation of DNA repair; transcription, DNA-dependent; negative regulation of transcription factor activity; pyrimidine dimer repair via nucleotide-excision repair; cell aging; negative regulation of I-kappaB kinase/NF-kappaB cascade; ovulation from ovarian follicle; cellular response to starvation; negative regulation of fat cell differentiation; regulation of endodeoxyribonuclease activity; cholesterol homeostasis; protein amino acid ADP-ribosylation; methylation-dependent chromatin silencing; inhibition of NF-kappaB transcription factor; maintenance of chromatin silencing; regulation of protein import into nucleus, translocation; negative regulation of phosphorylation; positive regulation of transcription from RNA polymerase II promoter; response to oxidative stress; triacylglycerol mobilization; negative regulation of transcription, DNA-dependent; rRNA processing; peptidyl-lysine acetylation; negative regulation of apoptosis; chromatin silencing at rDNA; proteasomal ubiquitin-dependent protein catabolic process; establishment of chromatin silencing; chromatin silencing; negative regulation of transcription from RNA polymerase II promoter; regulation of gene expression, epigenetic; response to insulin stimulus; DNA synthesis during DNA repair; protein amino acid deacetylation; positive regulation of MHC class II biosynthetic process; positive regulation of cell proliferation; angiogenesis; circadian regulation of gene expression; DNA replication; DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis; positive regulation of chromatin silencing; single strand break repair; negative regulation of TOR signaling pathway; negative regulation of protein kinase B signaling cascade; protein destabilization; histone deacetylation; DNA repair; regulation of cell proliferation; negative regulation of helicase activity; response to hydrogen peroxide; fatty acid homeostasis; white fat cell differentiation; cell glucose homeostasis; spermatogenesis; gene expression; positive regulation of protein amino acid phosphorylation; positive regulation of insulin receptor signaling pathway; negative regulation of cell growth; negative regulation of transforming growth factor beta receptor signaling pathway; response to DNA damage stimulus; positive regulation of macroautophagy