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SKU:PB9159
Pack Size:100μg/vial
Sample Size:30ug for $99, contact us for details
Clonality:Polyclonal
Application:WB
Price: $240.00
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Overview

Product Name Anti-SIRT1/Sirtuin 1 Picoband™ Antibody
SKU/Catalog Number PB9159
Description Rabbit IgG polyclonal antibody for NAD-dependent protein deacetylase sirtuin-1(SIRT1) detection. Tested with WB in Human.
Cite This Product Anti-SIRT1/Sirtuin 1 Picoband™ Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PB9159)
Replacement Item This antibody may replace the following items: sc-15404|sc-19857|sc-19858|sc-74465|sc-74504|sc-135792|sc-135791 from Santa Cruz Biotechnology.
Host Rabbit
Isotype N/A
Validated Species Human
Application WB

*Our Boster Guarantee covers the use of this product in the above tested applications.

**For positive and negative control design, consult "Tissue specificity" under Protein Target Info.

Recommended Detection Systems Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot.
*Blocking peptide can be purchased at $50. Contact us for more information
**Boster also offers various secondary antibodies for Immunoflourescecne and IHC. Take advantage of the buy 1 primary antibody get 1 secondary antibody for free promotion for the entire year 2017!
Immunogen E.coli-derived human SIRT1 recombinant protein (Position: R112-K311). Human SIRT1 shares 90% amino acid (aa) sequence identity with mouse SIRT1.
Cross Reactivity No cross reactivity with other proteins
Pack Size 100μg/vial

Properties

Clonality Polyclonal
Form Lyophilized
Contents Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.
*carrier free antibody available upon request.
Concentration Add 0.2ml of distilled water will yield a concentration of 500ug/ml.
Storage At -20˚C for one year. After reconstitution, at 4˚C for one month. It can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing.
Purification Immunogen affinity purified.
Isotype N/A

Protein Target Info (Source: Uniprot.org)

You can check the tissue specificity below for information on selecting positive and negative control.

Gene Name SIRT1
Protein Name NAD-dependent protein deacetylase sirtuin-1
Molecular Weight 81681 MW
Protein Function NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metobolism, apoptosis and autophagy. Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression. 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. Is 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. 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. Deacetylates 'Lys-266' of SUV39H1, leading to its activation. Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. Deacetylates H2A and 'Lys-26' of HIST1H1E. Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression. Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting. Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1. Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2. This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response. Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence. Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability. Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation. Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis. Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing. Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha. Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1. Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver. Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation. Involved in HES1- and HEY2-mediated transcriptional repression. In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62'. Deacetylates MEF2D. Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3. Represses HNF1A- mediated transcription. Required for the repression of ESRRG by CREBZF. Modulates AP-1 transcription factor activity. Deacetylates NR1H3 AND NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteosomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed. Involved in lipid metabolism. Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2. Deacetylates ACSS2 leading to its activation, and HMGCS1. Involved in liver and muscle metabolism. Through deacteylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletel muscle under low-glucose conditions and is involved in glucose homeostasis. Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression. Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and faciliting recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2. Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN. Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage. Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1. Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8. Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation. Proposed to play role in regulation of STK11/LBK1- dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear. In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability. Deacteylates MECOM/EVI1. Isoform 2 is shown to deacetylate 'Lys-382' of p53/TP53, however with lower activity than isoform 1. In combination, the two isoforms exert an additive effect. Isoform 2 regulates p53/TP53 expression and cellular stress response and is in turn repressed by p53/TP53 presenting a SIRT1 isoform-dependent auto-regulatory loop. In case of HIV-1 infection, interacts with and deacetylates the viral Tat protein. The viral Tat protein inhibits SIRT1 deacetylation activity toward RELA/NF-kappa-B p65, thereby potentiates its transcriptional activity and SIRT1 is proposed to contribute to T- cell hyperactivation during infection. Deacetylates PML at 'Lys- 487' and this deacetylation promotes PML control of PER2 nuclear localization. During the neurogenic transition, repress selective NOTCH1-target genes through histone deacetylation in a BCL6- dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including ARNTL/BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling. Deacetylates ARNTL/BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator. Deacetylates PER2, facilitating its ubiquitination and degradation by the proteosome. Protects cardiomyocytes against palmitate-induced apoptosis (PubMed:11672523, PubMed:12006491, PubMed:14976264, PubMed:14980222, PubMed:15126506, PubMed:15152190, PubMed:15205477, PubMed:15469825, PubMed:15692560, PubMed:16079181, PubMed:16166628, PubMed:16892051, PubMed:16998810, PubMed:17283066, PubMed:17334224, PubMed:17505061, PubMed:17612497, PubMed:17620057, PubMed:17936707, PubMed:18203716, PubMed:18296641, PubMed:18662546, PubMed:18687677, PubMed:19188449, PubMed:19220062, PubMed:19364925, PubMed:19690166, PubMed:19934257, PubMed:20097625, PubMed:20100829, PubMed:20203304, PubMed:20375098, PubMed:20620956, PubMed:20670893, PubMed:20817729, PubMed:20975832, PubMed:21149730, PubMed:21245319, PubMed:21471201, PubMed:21504832, PubMed:21555002, PubMed:21698133, PubMed:21701047, PubMed:21775285, PubMed:21807113, PubMed:21841822, PubMed:21890893, PubMed:21909281, PubMed:21947282, PubMed:22274616). Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity (PubMed:20955178). Involved in the CCAR2-mediated regulation of PCK1 and NR1D1 (PubMed:24415752). Deacetylates CTNB1 at 'Lys-49' (PubMed:24824780). {ECO:0000250

UniProtKB:Q923E4, ECO:0000269

PubMed:11672523, ECO:0000269

PubMed:12006491, ECO:0000269

PubMed:14976264, ECO:0000269

PubMed:14980222, ECO:0000269

PubMed:15126506, ECO:0000269

PubMed:15152190, ECO:0000269

PubMed:15205477, ECO:0000269

PubMed:15469825, ECO:0000269

PubMed:15692560, ECO:0000269

PubMed:16079181, ECO:0000269

PubMed:16166628, ECO:0000269

PubMed:16892051, ECO:0000269

PubMed:16998810, ECO:0000269

PubMed:17283066, ECO:0000269

PubMed:17290224, ECO:0000269

PubMed:17334224, ECO:0000269

PubMed:17505061, ECO:0000269

PubMed:17612497, ECO:0000269

PubMed:17620057, ECO:0000269

PubMed:17936707, ECO:0000269

PubMed:18203716, ECO:0000269

PubMed:18296641, ECO:0000269

PubMed:18662546, ECO:0000269

PubMed:18687677, ECO:0000269

PubMed:19188449, ECO:0000269

PubMed:19220062, ECO:0000269

PubMed:19364925, ECO:0000269

PubMed:19690166, ECO:0000269

PubMed:19934257, ECO:0000269

PubMed:20097625, ECO:0000269

PubMed:20100829, ECO:0000269

PubMed:20203304, ECO:0000269

PubMed:20375098, ECO:0000269

PubMed:20620956, ECO:0000269

PubMed:20670893, ECO:0000269

PubMed:20817729, ECO:0000269

PubMed:20955178, ECO:0000269

PubMed:20975832, ECO:0000269

PubMed:21149730, ECO:0000269

PubMed:21245319, ECO:0000269

PubMed:21471201, ECO:0000269

PubMed:21504832, ECO:0000269

PubMed:21555002, ECO:0000269

PubMed:21698133, ECO:0000269

PubMed:21701047, ECO:0000269

PubMed:21775285, ECO:0000269

PubMed:21807113, ECO:0000269

PubMed:21841822, ECO:0000269

PubMed:21890893, ECO:0000269

PubMed:21909281, ECO:0000269

PubMed:21947282, ECO:0000269

PubMed:22274616, ECO:0000269

PubMed:24415752, ECO:0000269

PubMed:24824780}.
Tissue Specificity Widely expressed. .
Sequence Similarities Belongs to the sirtuin family. Class I subfamily.
Subcellular Localization Nucleus, PML body. Cytoplasm. Nucleus . Recruited to the nuclear bodies via its interaction with PML. Colocalized with APEX1 in the nucleus. May be found in nucleolus, nuclear euchromatin, heterochromatin and inner membrane. Shuttles between nucleus and cytoplasm (By similarity). Colocalizes in the nucleus with XBP1 isoform 2 (PubMed:20955178). .
Uniprot ID Q96EB6
Alternative Names NAD-dependent protein deacetylase sirtuin-1;hSIRT1;3.5.1.-;Regulatory protein SIR2 homolog 1;SIR2-like protein 1;hSIR2;SirtT1 75 kDa fragment;75SirT1;SIRT1;SIR2L1;
Research Areas |cell biology|apoptosis|intracellular|p53 pathway| epigenetics and nuclear signaling|chromatin modifying enzymes|acetylation| microbiology|interspecies interaction|host virus interaction| tags & cell markers|subcellular markers|nucleus|other nuclear bodies|hdacs|class iii / sir2 class| metabolism|types of disease|obesity|
*if product is indicated to react with multiple species, protein info is based on the human gene.

Background for NAD-dependent protein deacetylase sirtuin-1

Sirtuin 1, also known as SIR2L1 or SIRT1, is a protein that in humans is encoded by the SIRT1 gene. It is mapped to 10q21.3. Sirtuin 1 is a member of the sirtuin family of proteins, homologs of the Sir2 gene in S. cerevisiae. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. Sirtuin 1 is downregulated in cells that have high insulin resistance and inducing its expression increases insulin sensitivity, suggesting the molecule is associated with improving insulin sensitivity. Furthermore, Sirtuin 1 was shown to de-acetylate and affect the activity of both members of the PGC1-alpha/ERR-alpha complex, which are essential metabolic regulatory transcription factors.

Anti-SIRT1/Sirtuin 1 Picoband™ Antibody Images

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Anti-SIRT1/Sirtuin 1 Picoband™ Antibody
Anti-SIRT1 Picoband antibody, PB9159-1.jpg
All lanes: Anti SIRT1 (PB9159) at 0.5ug/ml
WB: Recombinant Human SIRT1 Protein 0.5ng
Predicted bind size: 39KD
Observed bind size: 39KD
Anti-SIRT1/Sirtuin 1 Picoband™ Antibody
Anti-SIRT1 Picoband antibody, PB9159-2.jpg
All lanes: Anti SIRT1 (PB9159) at 0.5ug/ml
Lane 1: HEPG2 Whole Cell Lysate at 40ug
Lane 2: MCF Whole Cell Lysate at 40ug
Lane 3: SW620 Cell Lysate at 40ug
Predicted bind size: 120KD
Observed bind size: 120KD
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Publications

Hou S, Zheng F, Li Y, Gao L, Zhang J. Int J Mol Sci. 2014 Aug 26;15(9):15026-43. Doi: 10.3390/Ijms150915026. The Protective Effect Of Glycyrrhizic Acid On Renal Tubular Epithelial Cell Injury Induced By High Glucose.

FAQs

Q: Do you offer BSA-free antibodies? Keyword: Bovine serum albumin, carrier protein, conjugation
A: Yes, please contact us at support@bosterbio.com for more information about BSA-free antibodies and availability. The new BSA-free formula uses trehalose as a replacement to BSA. We have tested many alternative chemicals and found that trehalose protects the antibodies the best.
Q: Can I conjugate markers to this antibody? Can I link custom conjugates to this antibody? Keyword: conjugation
A: The antibody is stored with BSA and cannot be conjugated with markers. Carrier free antibodies are available upon request. Please contact support@bosterbio.com
Q: What should I use for negative control?
A: Please contact us for negative control suggestions. You can also check expression databases such as genecards, uniprot etc. Due to logistic reasons, we do not sell serum or lysates that we use internally for positive or negative control.
Q: Where can I find troubleshooting information? What should I do if I have unexpected bands, high background, no signal, weak signal
A: You can find Boster's troubleshoot guides under tech support tab. Please contact us for further assistance on troubleshooting your experiment.
Q: What is the immunogen sequence of this antibody? Is this antibody polyclonal or monoclonal?
A: You can find the immunogen sequence under "Immunogen" and clonality in the product name.
Q: What is the expected band size? Why is it different than the observed band size?
A: The expected band size is predicted on the size of the protein. The actual band size may be affected by a few other factors including but not limited to:
1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands

3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.

4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,
Q: What is the suggested dilution ratio for Western Blot (WB), Immunohistochemistry (IHC) and or ELISA standards? What is the optimal pH for the sample?
A: Check the datasheet for the product for details on dilution ratios for different experiments. You can find the datasheet button on the right side of the product page.
Q: What is the protocol you used for your Western blotting (WB) and Immunohistochemistry (IHC)?
A: Check our protocols under the tech support tab.
Q: What are some alternative names that could be used to describe this product?
A: Some common names include but are not limited to sirt1 antibody, sirtuin 1 antibody