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Validated All-in-One™ qPCR Primer for SIRT1(NM_012238.4) Search again
Product ID:
HQP088631
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
SIR2, SIR2L1, SIR2alpha
Gene Description:
sirtuin 1
Target Gene Accession:
NM_012238.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
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].
Gene References into function
- SIRT1(Sir2alpha) deacetylates p53 and promotes survival
- the SIRT1 deacetylase as a novel negative regulator of p53 function capable of modulating cellular senescence
- Data show that physiological concentrations of nicotinamide noncompetitively inhibit SIRT1 in vitro.
- These results indicate that the molecular association between HES1-, HEY2- and SIRT1-related proteins is conserved among metazoans, from Drosophila to human, and suggest that the Sir2-bHLH interaction also plays important roles in human cells.
- SIRT1 is a histone H3/H4 deacetylase in mammalian cells and in transcriptional repression mediated by CTIP2
- SIRT1 and FOXO3 formed a complex in cells in response to oxidative stress; SIRT1 deacetylated FOXO3; SIRT1 increased FOXO3's ability to induce cell cycle arrest and resistance to oxidative stress but inhibited FOXO3's ability to induce cell death
- SIRT1 represses forkhead transcription factors and reduces apoptosis
- Data demonstrate that acetylation functions in a second pathway of negative control for FOXO factors and provides a novel mechanism whereby hSir2(SIRT1) can promote cellular survival and increase lifespan.
- provides evidence that SIRT1 activity augments apoptosis in response to TNFalpha by the ability of the deacetylase to inhibit the transactivation potential of the RelA/p65 protein
- SIRT1 deacetylates the DNA repair factor Ku70, causing it to sequester the proapoptotic factor Bax away from mitochondria, thereby inhibiting stress-induced apoptotic cell death
- SIRT1 deacetylation and repression of p300 involves specific lysine residues in the cell cycle regulatory domain 1
- SIRT1 has a role in transcriptional repression mediated by BCL11A in mammalian cells
- substrate recognition by SIRT1 does not depend on the amino acid sequence proximate to the acetylated lysine
- FHL2 inhibits FOXO1 activity in prostate cancer cells by promoting the deacetylation of FOXO1 by SIRT1
- Hiv Tat is deacetylated by human sirtuin 1 (SIRT1), a nicotinamide adenine dinucleotide-dependent class III protein deacetylase in vitro and in vivo
- binding of resveratrol to SIRT1 promotes a conformational change that accommodates the attached coumarin group
- histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications regulate MEF2
- SIRT1 protects against microglia-dependent amyloid-beta toxicity through inhibiting NF-kappaB signaling
- PARP activation and the concomitant reduction of Sir2alpha activity in failing hearts regulate the post-translational acetylation of p53
- Overexpression of sirt1 induced expression of P-glycoprotein and rendered cancer cells resistant to doxorubicin.
- Data describe the cloning, chromosomal characterization and mapping of the NAD-dependent histone deacetylases gene sirtuin 1.(
- Although SIRT1 deacetylates p53, this does not play a role in cell survival following DNA damage in certain cell lines and primary human mammary epithelial cells.
- AIF-mediated cell death is regulated by the functional interplay of SIRT1 and PARP-1 in response to DNA damage
- expression of SIRT1 in the brain resulted in decreased ROCK1 expression and elevated alpha-secretase activity; SIRT1 activation in the brain is a novel mechanism through which calorie restriction may influence Alzheimer disease amyloid neuropathology
- There is a mutual regulation between E2F1 and SirT1 that affects cellular sensitivity to DNA damage.
- evidence for an androgen receptor (AR) regulatory pathway controlled by SIRT1; SIRT1 antagonists induce endogenous AR expression and enhance dihydrotestosterone-mediated AR expression
- SIRT1 can modulate p73 activity via deacetylation.
- SIRT1 regulates cigarette smoke induced pro-inflammatory mediators release via RelA/p65 NF-{kappa}B in macrophages.
- These data show that SIRT1 regulates cigarette smoke-mediated proinflammatory mediator release via NF-kappaB, implicating a role of SIRT1 in sustained inflammation and aging of the lungs.
- In contrast, a SIRT1 inhibitory compound showed a stimulatory activity on the differentiation of adipocytes, a feature often linked to insulin sensitization.
- The association of three Sirt1 SNPs and energy homeostasis in Finnish subjects implicates SIRT1 as a key regulator of energy and metabolic homeostasis.
- Overexpression of SIRT1 may have some relevance to the early stage of skin carcinogenesis.
- propose that the reduction in transcriptional repression mediated by hypermethylated in cancer 1, due to the decrease of CtBP binding, increases SIRT1 expression
- HIC1 is a target of the class III deacetylase SIRT1 and identify a new posttranslational modification step in the P53-HIC1-SIRT1 regulatory loop.
- HuR regulates SIRT1 expression, underscore functional links between the two stress-response proteins, and implicate Chk2 in these processes.
- SIRT1 modulates DNA repair activity, which could be regulated by the acetylation status of repair protein Ku70 following DNA damage
- Corepressor of androgen receptor, elucidating a new pathway relevant to prostate cancer growth and approaches to therapy.
- SIRT1 was distributed in cytoplasm at metaphase during mitosis, and overexpression of SIRT1 significantly augmented apoptosis for cells at metaphase.
- SIRT1 constitutes a unique molecular link between aging and human neurodegenerative disorders and provides a promising avenue for therapeutic intervention
- Deacetylation of NBS1 by SIRT1 plays a key role in the dynamic regulation of the DNA damage response and in the maintenance of genomic stability.
- downregulation of Sirt1 decreases survival and increases radiation-induced antiproliferation effects of human lung cancer cells
- SIRT1 is significantly elevated in mouse and human prostate cancer
- interaction between Sirt1 and TLE1 is important for mediating repression of NF-kappaB activity
- SIRT1 promotes endothelium-dependent vascular relaxation by activating eNOS.
- Data show that SIRT1 is highly expressed in cancer cell lines as well as in tissue samples from colon carcinoma patients.
- SIRT1 haplotypes were assessed for association with the risks of mortality, metabolic profile, age-related diseases, and cognitive functioning. These analyses revealed a trend for lower cardiovascular mortality for haplotype 2 and rs3758391 SNP carriers.
- possible regulatory effect of SirT1 on insulin-induced tyrosine phosphorylation of IRS-2, a vital step in insulin signaling pathway, through deacetylation of IRS-2 protein.
- Sirt1 exerts a protective effects against endothelial dysfunction by preventing stress-induced premature senescence.
- A novel post-translational sumoylation of SIRT1 at Lys734 increased its deacetylase activity. Stress-inducing agents promoted association of SIRT1 with SENP1 and cells depleted of SENP1 were more resistant to stress-induced apoptosis.
- Activation of the SIRT1/PGC-1 pathway, in a metabolic context promotes mitochondrial function and this pathway plays a role in neurodegerative disease. Review.
- Active regulator of SIRT1 (AROS) is the first direct SIRT1 regulator to be identified that modulates p53-mediated growth regulation.
- SIRT1 protein may be functionally associated with WRN and BLM helicases and that some major SIRT1 functions may not require its deacetylase activity.
- SIRT1 plays a pivotal role in regulation of NF-kappaB-dependent proinflammatory mediators in lungs of smokers and patients with COPD.
- Inhibition of SIRT1 in telomerase-immortalized human cells and hematopoietic stem cells obtained from SIRT1-deficient mice enhanced cell growth under normal and nutrient limiting conditions.
- SIRT1 can function as a growth suppressor and regulates AMPK and Telomerase
- SIRT1 regulates WRN-mediated cellular responses to DNA damage through deacetylation of WRN.
- Our results indicate that nicotinamide treatment attenuates p21WAF1 expression through Sp1 downregulation, and suggest a possible involvement of nicotinamide metabolism in cellular gene expression.
- DBC1 directly interacts with SIRT1 and inhibits SIRT1 activity in vitro and in vivo
- DBC1 (deleted in breast cancer 1) acts as a native inhibitor of SIRT1 in human cells
- results suggest that the Sirt1 deacetylase is an important in vivo regulator of autophagy and provide a link between sirtuin function and the overall cellular response to limited nutrients.
- These results support a model where the normal function of SIRT1 as a negative regulator of T cell activation is suppressed by Tat during HIV infection.
- SIRT1 suppresses intestinal tumor formation in vitro
- SIRT1 functions as a novel upstream regulator for LKB1/AMP-activated protein kinase signaling and plays an essential role in the regulation of hepatocyte lipid metabolism
- Sirt1 overexpression rescued H(2)O(2)-induced apoptosis through the upregulation of catalase.
- Cilostazol inhibits oxidative stress-induced premature senescence via upregulation of Sirt1 in human endothelial cells.
- SIRT1 functions in normal human keratinocytes to inhibit proliferation and to promote differentiation
- These results suggest that up-regulation of SIRT1 expression may play an important role in promoting cell growth and chemoresistance in androgen-refractory prostate cancer cells.
- LKB1 deacetylation is regulated by SIRT1 and that this in turn influences its intracellular localization, association with STRAD, kinase activity, and ability to activate AMPK.
- Endothelium-specific overexpression of class III deacetylase SIRT1 decreases atherosclerosis in apolipoprotein E-deficient mice.
- During the DNA break, SIRT1 recruits the DNMT3B and causes methylation of the promoter in the silent clones.
- Overexpression of SIRT1 isassociated with cisplatin resistance in cancer cells by altering mitochondrial metabolism.
- SIRT1 expression is associated with poor prognosis of diffuse large B-cell lymphoma.
- miR-34a functions as a tumor suppressor, in part, through a SIRT1-p53 pathway
- In this review they outline recent research advances on the regulation of SIRT1 which may provide the basis for the development of therapeutic inhibitors with improved specificity.
- Single nucleotide polymorphism in SIRT1 gene is associated with visceral obesity.
- A growing body of evidence suggests a role of SIRT1 in maintaining energy and nutrient homeostasis, thereby linking its anti-aging property to its role in metabolism--REVIEW
- A previously unrecognized role is suggested for brain SIRT1 in regulating energy homeostasis.
- Reporter assays revealed that miR-34a-induced SIRT1 inhibition occurred at the transcriptional but not post-transcriptional level despite the presence of a potential miR-34a binding site within its 3'-UTR.
- Show that many human cancers exhibit reduced levels of SIRT1 compared to normal controls.
- that elevated SIRT1 protein in human cells is not attributable to increased SIRT1 mRNA levels but, instead, reflects SIRT1 protein stability.
- Deacetylation of cortactin is associated with high levels of SIRT1 and tumorigenesis.
- cartilage-specific gene expression in human chondrocytes is regulated by SirT1 and nicotinamide phosphoribosyltransferase
- A novel chalcone polyphenol inhibits the deacetylase activity of SIRT1 and cell growth in HEK293T cells.
- SIRT1 genetic variants may represent a relevant determinant for the response rate of individuals undergoing caloric restriction and increased physical activity
- The implications of SIRT1 as a therapeutic target for the optimal balance between anti-aging and anti-cancer activities.
- These findings raise the possibility that glucose-induced changes in AMPK are linked to alterations in SIRT1 abundance and activity and possibly cellular redox state.
- The seemingly opposite oncogenic and tumour-suppressive effects of SIRT1 depends on the status of p53.
- the cellular regulation of SIRT1 expression and activity[Review]
- results provide a mechanistic basis for the requirement of HSF1 in the regulation of life span and establish a role for SIRT1 in protein homeostasis and the heat shock response