Anti sirt7

Manufactured by Cell Signaling Technology

Sourced in United States, Poland

Anti-Sirt7 is a primary antibody that recognizes the Sirt7 protein. Sirt7 is a member of the sirtuin family of NAD-dependent deacetylases, which play important roles in cellular processes such as gene expression, metabolism, and stress response. The Anti-Sirt7 antibody can be used to detect and study the expression and localization of Sirt7 in various experimental systems.

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SIRT7 (7 citations) Anti-SIRT7 (5360), (2 citations)

6 protocols using anti sirt7

Protein Expression Profiling of Rapha Myr-Treated Cells

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Whole cell protein of untreated and 24 h Rapha Myr^® extract (0.5–1.25–2.5% v/v)-treated cells were prepared according to Laemmli (1970) and submitted to Western blot analysis, performed according to Grabowska et al., 2016 [72 (link)]. The primary antibodies used were: anti-integrin α5 (1:1000) (Immunological Sciences, Rome, Italy), anti-GAPDH (1:50,000) (Millipore, Darmstadt, Germany), anti-Poly (ADP-ribose)polymerase (PARP, 1:1000) (BD Biosciences, San Jose, CA, USA), anti-γH2AX Ser139 (1:1000) (Abcam, Cambridge, UK), anti-p53 (1:500) (Santa Cruz Biotechnology, Santa Cruz, CA, USA), anti-p21 (1:500) (Sigma-Aldrich, St. Louis, MO, USA), anti-phospho-p53 Ser15 (1:250), anti-sirt 1 (1:250), anti-phospho-sirt 1 Ser47 (1:250), anti-sirt 3 (1:500), anti-sirt 5 (1:500), anti-sirt 6 (1:1000) and anti-sirt 7 (1:250) (Cell Signalling Technology, Denvers, CO, USA). Each protein target was detected by using specific secondary horseradish peroxidase-conjugated antibodies (1:2000) (Dako, Glostrup, Denmark) and an ECL system (Thermo Scientific, Rockford, IL, USA). The expression level of proteins was measured by densitometric analysis using the software Image J and GAPDH was chosen as the reference protein.

Tomasello B., Di Mauro M.D., Malfa G.A., Acquaviva R., Sinatra F., Spampinato G., Laudani S., Villaggio G., Bielak-Zmijewska A., Grabowska W., Barbagallo I.A., Liuzzo M.T., Sbisà E., Forte M.G., Di Giacomo C., Bonucci M, & Renis M. (2020). Rapha Myr®, a Blend of Sulforaphane and Myrosinase, Exerts Antitumor and Anoikis-Sensitizing Effects on Human Astrocytoma Cells Modulating Sirtuins and DNA Methylation. International Journal of Molecular Sciences, 21(15), 5328.

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Immunoblot Analysis of NF-κB Pathway Components

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Protein extracts were resolved by SDS-PAGE, transferred onto an Immunobilon membrane, and analyzed by immunoblot with the following specific antibodies: anti-p105/p50 (ab32360, 1:5000), anti-NF-κB p65 (RelA) (ab16502, 1:5000), anti-p300 (ab3164, 1:1000), anti-HDAC2 (ab7029, 1:1000), anti-Sirt1 (ab110304, 1:1000; all from Abcam); anti-p100/p52 (4882, 1:1000), anti-RelB (4922, 1:1000), anti-Histone H3 (4499, 1:2000), anti-β-actin (12262, 1:2000), anti-Batf (8638, 1:1000), anti-PU.1 (2258, 1:1000), anti-Phospho-STAT5 (9359, 1:1000), anti-Smad2 (5339, 1:1000), anti-Phospho-Smad2 (3108, 1:1000), anti-Smad3 (9523, 1:1000), anti-Phospho-Smad3 (9520, 1:1000), anti-Sirt7 (5360, 1:1000), anti-HDAC1 (2062, 1:1000; all from Cell Signaling Technology); and anti-STAT5 (SC-835X, 1:3000), anti-STAT6 (SC-981X, 1:4000), anti-phospho-STAT6 (SC-11762X, 1:3000), anti-IRF4 (sc-6059, 1:1000; all from Santa Cruz Technology). Horseradish peroxidase (HRP)–linked antibody to mouse IgG (7076, 1:2000), HRP–linked antibody to rabbit IgG (7074, 1:2000; both from Cell Signaling Technology) and HRP–linked antibody to goat IgG (sc-2768, 1:2000; Santa Cruz Technology) were used as secondary antibodies. The expression of target molecules was detected by chemoluminescence method. Images has been cropped for presentation; full-size immunoblots are provided in Supplementary Figure 7.

Xiao X., Shi X., Fan Y., Zhang X., Wu M., Lan P., Minze L., Fu Y.X., Ghobrial R.M., Liu W, & Li X.C. (2015). GITR subverts Foxp3+ Tregs to boost Th9 immunity through regulation of histone acetylation. Nature Communications, 6, 8266.

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Analysis of p53 Signaling in Cancer Cells

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p53^+/+ HCT116 and p53^−/− HCT116 (human colon cancer) and U2OS (human osteosarcoma cancer) cell lines were cultured in DMEM (HyClone SH30243.01) supplemented with 10% (vol/vol) fetal bovine serum (FSP500) and 1% (vol/vol) penicillin/streptomycin (HyClone CC004) and maintained in a humidified 37 °C incubator with a 5% (vol/vol) CO₂ atmosphere. HC116 and U2OS cell lines both acquired from ATCC. For glucose starvation, cells were cultured in DMEM no glucose medium (Gibco 11966-025). The antibodies used in this study included: anti-p21 (Cell Signaling 2947S), anti-SIRT7 (Cell Signaling 5360S), anti-acetyl-lysine (Cell Signaling 9441S), anti-p53 (DO-1 sc-126), anti-β-actin (Santa Cruz 3700S), anti-PCAF (Bethyl and Cell Signaling 3378S), anti-MDM2 (ab16895 and Cell Signaling 86934), anti-FLAG (Sigma F1804), and anti-MYC (MBL M047-3). MG132 was purchased from Sigma (M7449) and CHX was purchased from Cell Signaling (2112S).

Lu Y.F., Xu X.P., Lu X.P., Zhu Q., Liu G., Bao Y.T., Wen H., Li Y.L., Gu W, & Zhu W.G. (2020). SIRT7 activates p53 by enhancing PCAF-mediated MDM2 degradation to arrest the cell cycle. Oncogene, 39(24), 4650-4665.

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Immunoblot Analysis of Protein Signaling

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Protein extracts were resolved by SDS–PAGE, transferred onto an Immunobilon membrane, and analysed by immunoblot with the following specific antibodies: anti-p105/p50 (ab32360, 1:5,000), anti-NF-κB p65 (RelA) (ab16502, 1:5,000), anti-p300 (ab3164, 1:1,000), anti-HDAC2 (ab7029, 1:1,000), anti-Sirt1 (ab110304, 1:1,000; all from Abcam); anti-p100/p52 (4882, 1:1,000), anti-RelB (4922, 1:1,000), anti-Histone H3 (4499, 1:2,000), anti-β-actin (12262, 1:2,000), anti-Batf (8638, 1:1,000), anti-PU.1 (2258, 1:1,000), anti-Phospho-STAT5 (9359, 1:1,000), anti-Smad2 (5339, 1:1,000), anti-Phospho-Smad2 (3108, 1:1,000), anti-Smad3 (9523, 1:1,000), anti-Phospho-Smad3 (9520, 1:1,000), anti-Sirt7 (5360, 1:1,000), anti-HDAC1 (2062, 1:1,000; all from Cell Signaling Technology); and anti-STAT5 (SC-835X, 1:3,000), anti-STAT6 (SC-981X, 1:4,000), anti-phospho-STAT6 (SC-11762X, 1:3,000), anti-IRF4 (sc-6059, 1:1,000; all from Santa Cruz Technology). Horseradish peroxidase (HRP)-linked antibody to mouse IgG (7076, 1:2,000), HRP–linked antibody to rabbit IgG (7074, 1:2,000; both from Cell Signaling Technology) and HRP-linked antibody to goat IgG (sc-2768, 1:2,000; Santa Cruz Technology) were used as secondary antibodies. The expression of target molecules was detected by chemoluminescence method. Images has been cropped for presentation; full-size immunoblots are provided in Supplementary Fig. 7.

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Protein Extraction and Western Blot Analysis

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Whole cell protein extracts were prepared according to Laemmli (Laemmli 1970 (link)). The primary antibodies used were the following: anti-ATM (1:500), anti-phospho-ATM Ser1981 (1:500), and anti-GAPDH (1:50,000) (Millipore, Warsaw, Poland); anti-p53 (1:500), anti-p21 (1:500), and anti-p16 (1:250) (Santa Cruz Biotechnology, Santa Cruz, USA); anti-phospho-p53 Ser15 (1:250) (Becton Dickinson, Warsaw, Poland); anti-HO-1 (1:1000) (Enzo Life Sciences, Warsaw, Poland); SIRT1 (1:250), phospho-SIRT1 Ser47 (1:250), anti-SIRT2 (1:1000), anti-SIRT3 (1:500), anti-SIRT5 (1:500), anti-SIRT6 (1:1000), anti-SIRT7 (1:250), anti-phospho-p38 Thr180/Tyr182 (1:500), and anti-p38 (1:500) (Cell Signaling Technology, Poznań, Poland); and anti-AGTR1 (1:500) and anti-actin (1:50,000) (Sigma-Aldrich, Poznan, Poland). The respective proteins were detected after incubation with one of the horseradish peroxidase-conjugated secondary antibodies (1:2000) (Dako, Gdynia, Poland), using an ECL system (Thermo Scientific, Warsaw, Poland), according to the manufacturer’s instructions.

Grabowska W., Kucharewicz K., Wnuk M., Lewinska A., Suszek M., Przybylska D., Mosieniak G., Sikora E, & Bielak-Zmijewska A. (2015). Curcumin induces senescence of primary human cells building the vasculature in a DNA damage and ATM-independent manner. Age, 37(1), 7.

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Co-immunoprecipitation and Western Blot Analysis

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Co-immunoprecipitation experiments were performed as described [19,21] in presence of 0.15 U/µL of benzonase (Sigma-Aldrich) using ANTI-FLAG® M2 Affinity Gel (Sigma-Aldrich) followed by elution with FLAG®-peptide (Sigma-Aldrich) or with Anti-Tag (CGY)FP (Evrogen) and anti-Suv39h1 antibody (Novus Biologicals), as indicated. Western blotting was performed as described [19] using the following primary antibodies: ANTI-FLAG® M2 (Sigma-Aldrich), Anti-Tag (CGY)FP (Evrogen), Anti-Sirt7 (Cell Signaling Technology), Anti-Sirt1 (Cell Signaling Technology), Anti-H3K9me3 (Abcam), Anti-RalA (BD Trans. Laboratories; R23520), Anti-Histone 3 (Cell Signaling Technology), anti-HA.11 Tag antibody (Biolegend), anti-Suv39h1 (Cell Signaling Technology), and anti-Suv39h1 (Novus Biologicals). Quantification of the intensity of western blot signals was achieved using Image Lab™ 5.0 software (Bio-Rad).

Kumari P., Popescu D., Yue S., Bober E., Ianni A, & Braun T. (2018). Sirt7 inhibits Sirt1-mediated activation of Suv39h1. Cell Cycle, 17(12), 1403-1412.

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