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Supersignal chemiluminescence detection system

Manufactured by Thermo Fisher Scientific
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The SuperSignal Chemiluminescence Detection System is a lab equipment product used for the detection and quantification of chemiluminescent signals. It provides a sensitive and reliable method for analyzing a variety of biomolecules, including proteins, nucleic acids, and other targets.

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Lab products found in correlation

Horseradish peroxidase conjugated secondary antibody, by Jackson ImmunoResearch (2 mentions) Nanog, by Cell Signaling Technology (2 mentions) Aldh1, by Cell Signaling Technology (1 mentions) Complete mini protease inhibitor tablet, by Roche (1 mentions) Ab52857, by Abcam (1 mentions) Ab6789, by Abcam (1 mentions) Ab6721, by Abcam (1 mentions) Protease and phosphatase inhibitor, by Roche (1 mentions) Bca assay, by Thermo Fisher Scientific (1 mentions) Imagequant tl software, by GE Healthcare (1 mentions)

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SuperSignal West Pico Chemiluminescence Detection System SuperSignal West‐Femto Chemiluminescence detection system SuperSignal chemiluminescence system SuperSignal detection system Chemiluminescence detection system SuperSignal system Chemiluminescence system

6 protocols using supersignal chemiluminescence detection system

1

Western Blot Analysis of Stem Cell Markers

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The Western Blot protocol was performed as previously described (14). Briefly, 100μg of protein was loaded for H727 and H720 lysates. Oct-4, Sox-2, Nanog, CD44, ALDH1 (Cell Signaling Technology, Toronto, ON, Canada) antibodies were used at 1:1000 dilution. Secondary horseradish peroxidase conjugated antibodies (Jackson Immunoresearch, West Grove, PA, USA) were used at a dilution of 1:6000 and signal was detected with the Supersignal chemiluminescence detection system (Pierce Biotechnology, Rockford, IL, USA). GAPDH served as the loading control. Signals were quantified by densitometry relative to untreated values.
Bayat Mokhtari R., Baluch N., Morgatskaya E., Kumar S., Sparaneo A., Muscarella L.A., Zhao S., Cheng H.L., Das B, & Yeger H. (2019). Human bronchial carcinoid tumor initiating cells are targeted by the combination of acetazolamide and sulforaphane. BMC Cancer, 19, 864.
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2

Pluripotency Markers Expression Analysis

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Cells were lysed with RIPA extraction buffer (MBiotech, Seoul, Korea) supplemented with a CompleteMini protease inhibitor tablet (Roche, Indianopolis, IN, USA). 100ug of protein was loaded for SH-SY5Y lysates, and 20 μg for NT2/D1 lysates. OCT4, SOX2 (Cell Signaling Technology, Toronto, ON, Canada) and Nanog (Cell Signaling Technology, Toronto, ON, Canada) antibodies were used at 1/1000 dilution. Secondary horseradish peroxidase conjugated antibodies (Jackson Immunoresearch, West Grove, PA, USA) were used at a dilution of 1/6000 and signal was detected with the Supersignal chemiluminescence detection system (Pierce Biotechnology, Rockford, Il, USA).
Bayat Mokhtari R., Baluch N., Ka Hon Tsui M., Kumar S., S. Homayouni T., Aitken K., Das B., Baruchel S, & Yeger H. (2017). Acetazolamide potentiates the anti-tumor potential of HDACi, MS-275, in neuroblastoma. BMC Cancer, 17, 156.
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3

Protein Immunoprecipitation and Analysis

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Cells cultured in 150-mm diameter dishes were transfected using a calcium phosphate co-precipitation method with the plasmids indicated. Lysates were prepared two days post-transfection as previously described11 (link). Immunoprecipitations were performed using the standard technique, as in11 (link). Finally, the immunoprecipitated complexes were processed for SDS-PAGE and immunoblot analysis. Proteins were visualized by chemiluminescence using the SuperSignal Chemiluminescence Detection System (Thermo Fisher).
Forouzanfar F., Ali S., Wallet C., De Rovere M., Ducloy C., El Mekdad H., El Maassarani M., Aït-Ammar A., Van Assche J., Boutant E., Daouad F., Margottin-Goguet F., Moog C., Van Lint C., Schwartz C, & Rohr O. (2019). HIV-1 Vpr mediates the depletion of the cellular repressor CTIP2 to counteract viral gene silencing. Scientific Reports, 9, 13154.
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4

Protein Expression Analysis in Substantia Nigra and PC12 Cells

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Substantia nigra and PC12 cells were prepared in RIPA buffer containing protease and phosphatase inhibitors. Protein concentration was measured by BCA assay (Pierce). 20 μg of total protein from each sample was separated by SDS-PAGE (8%, 10% or 15%) and transferred to a PVDF membrane. After incubating in 0.01 M TBS, 0.1% Tween-20 and 5% non-fat dry milk powder for 1 h to block any remaining protein binding sites, membranes were incubated overnight at 4 °C using the following primary antibodies: the mouse antibody against TH (Sigma, SAB4200697, 1:2000), alpha-synuclein (Abcam, ab1903, 1:1000), β-tubulin (Proteintech,10,094–1-AP, 1:2000); the rabbit antibody against LC3, P62, Beclin-1, p-PI3K, PI3K, Sirt1 (Cell Signaling Technology, #4108, #5114, #3738, #4228, #4249, #9475, 1:1000) and FoxO1 (Abcam, ab52857, 1:1000). After three 5-min washes in TBST, membranes were incubated with the goat anti-mouse IgG H&L (HRP)/goat anti-rabbit IgG H&L (HRP) (Abcam, ab6789, ab6721, 1:2000) for 1 h at room temperature. All antibody incubations and washing steps were carried out in TBST. The immunoreactive blots were visualized using the supersignal chemiluminescence detection system (Thermo Fisher Scientific Inc.) and quantified with densitometry using ImageJ software.
Chen C., Xia B., Tang L., Wu W., Tang J., Liang Y., Yang H., Zhang Z., Lu Y., Chen G., Yang Y, & Zhao Y. (2018). Echinacoside protects against MPTP/MPP+-induced neurotoxicity via regulating autophagy pathway mediated by Sirt1. Metabolic Brain Disease, 34(1), 203-212.
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5

Cell Lysis and Western Blotting

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Cells were rinsed with ice-cold PBS, lysed with TNES buffer (50 mM Tris [pH 7.5], 2 mM EDTA, 100 mM NaCl, 1% NP-40) containing fresh protease and phosphatase inhibitor (Roche) and centrifuged at 4°C, 13,200 g for 30 minutes. Where applicable, soluble sample was removed and the insoluble pellet was rinsed with PBS following centrifugation. After pelleting and removal of PBS, TNES buffer was added and samples sonicated. All samples were quantified by BCA assay (Thermo). 10-20 μg of protein was separated by SDS-PAGE using Mini-PROTEAN TGX 4-20% precast gradient gels (BioRad), transferred to nitrocellulose membranes, blocked for 1 hour with TBS-T (50 mM Tris [pH 7.5], 300 mM NaCl, 0.5% Tween 20) containing 5% nonfat milk (blocking buffer), and incubated with primary antibody overnight at 4°C. The following day, membranes were rinsed in TBS-T and incubated with species-specific secondary antibody in blocking buffer for 1 hour at room temperature. Proteins were detected using the SuperSignal chemiluminescence detection system (Thermo) and films were scanned. The same blot was probed multiple times, and if necessary, was sliced horizontally for better exposure when the same antibody species was used. If brightness/contrast was adjusted, it was equivalently adjusted for the entire image. Antibodies used are listed in Supplemental Information.
Moses M.A., Kim Y.S., Rivera-Marquez G.M., Oshima N., Watson M.J., Beebe K.E., Wells C., Lee S., Zuehlke A.D., Shao H., Bingman WE I.I.I., Kumar V., Malhotra S.V., Weigel N.L., Gestwicki J.E., Trepel J.B, & Neckers L.M. (2018). Targeting the Hsp40/Hsp70 chaperone axis as a novel strategy to treat castration-resistant prostate cancer. Cancer research, 78(14), 4022-4035.
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6

Western Blot Analysis of Urinary Exosomes

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Urinary exosomal proteins were separated by SDS-PAGE (each sample was loaded in a lane with the same amount of creatinine) [22 (link),31 (link)] and then transferred to polyvinylidene difluoride membranes. After blocking with 5% skim milk in 0.05% Tween-Tris-buffered saline (TTBS), the membrane was incubated with 1.5% skim milk in TTBS including a primary antibody (anti-AQP2, -TSG101, or –ALIX antibody) at 30 °C for 1 h. The membrane was then incubated with 1.5% skim milk in TTBS including a secondary antibody at 30 °C for 45 min. Bands were visualized using a Super Signal chemiluminescence detection system (Thermo Fisher Scientific Inc., Waltham, MA, USA) and quantified using the ImageQuant TL software (GE Healthcare, Uppsala, Sweden). Corresponding control samples from animals treated with vehicle were always loaded in each gel for normalized quantification.
Abdeen A., Sonoda H., Kaito A., Oshikawa-Hori S., Fujimoto N, & Ikeda M. (2020). Decreased Excretion of Urinary Exosomal Aquaporin-2 in a Puromycin Aminonucleoside-Induced Nephrotic Syndrome Model. International Journal of Molecular Sciences, 21(12), 4288.
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