Supersignal west pico chemiluminescence reagent

Manufactured by Thermo Fisher Scientific

Sourced in United States

SuperSignal West Pico chemiluminescence reagent is a laboratory product manufactured by Thermo Fisher Scientific. The core function of this reagent is to produce a chemiluminescent signal for the detection of proteins in Western blot analysis.

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Lab products found in correlation

Electrotransfer apparatus, by Bio-Rad (2 mentions) Protein assay, by Bio-Rad (2 mentions) Nupage 4 12 bis tris mini gel, by Thermo Fisher Scientific (2 mentions) Protein assay dye reagent, by Bio-Rad (2 mentions) Nupage lds sample buffer, by Thermo Fisher Scientific (2 mentions) Nupage mes sds running buffer, by Thermo Fisher Scientific (2 mentions) Immobilon fl, by Merck Group (2 mentions) Triton x 100, by Merck Group (1 mentions) Tween 20, by Thermo Fisher Scientific (1 mentions) Tween 20, by Merck Group (1 mentions) Protease inhibitor cocktail, by Roche (1 mentions) Dc protein assay, by Bio-Rad (1 mentions) Iblot transfer stack, by Thermo Fisher Scientific (1 mentions) Snap i d system, by Merck Group (1 mentions) Horseradish peroxidase, by Abcam (1 mentions) α sma, by Abcam (1 mentions) Gapdh, by Thermo Fisher Scientific (1 mentions) Collagen 1, by Abcam (1 mentions) Sirt1, by Cell Signaling Technology (1 mentions) Bca protein assay kit, by Santa Cruz Biotechnology (1 mentions)

Close spelling variants of this product

SuperSignal West Pico (704 citations) Chemiluminescence reagent (164 citations) SuperSignal West Pico Chemiluminescence (15 citations) SuperSignal reagents (7 citations) Supersignal West Pico Chemiluminescence detection reagents (6 citations)

13 protocols using supersignal west pico chemiluminescence reagent

Western Blot Analysis of Protein Expression

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Transfectants were washed with PBS and lysed in distilled water containing 75
µl of 1.5% Triton X-100 (Sigma–Aldrich) with protease inhibitor
cocktail (Roche) per 10⁷ cells. Protein was determined by Dc protein assay
(Bio-Rad, Hercules, CA) and ∼50–100 μg protein electrophoresed
in a 10% Tris-HCl polyacrylamide gel at 10–30 mA for 2 hr. Transfer to
polyvinylidene difluoride (PerkinElmer, Inc.) membrane was performed overnight at 50
mA in buffer containing 10% methanol. Antibodies were diluted in Tris buffered saline
(10 mM Tris HCl, pH 7.4, 150 mM NaCl) containing 0.05% Tween 20 (Sigma Aldrich) and
3% nonfat dry milk supplemented with 3% BSA (Fraction V) or 3% nonfat dry milk,
respectively. Antibody dilutions were: anti-Myc mAb (9E10) 1:500, anti-HA mAb (HA.11)
1:1000, anti-beta actin mAb 1:5000, and HRP-conjugated goat anti-mouse secondary
antibody, 1:5000–10,000. After washing in Tris buffered saline containing
0.05% Tween 20, membrane was incubated with Super Signal West Pico chemiluminescence
reagent (Thermo Scientific) and exposed to film (Denville Scientific, Inc., South
Palinfield, NJ).

Huang H.H., Hassinen A., Sundaram S., Spiess A.N., Kellokumpu S, & Stanley P. (2015). GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain. eLife, 4, e08916.

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Western Blot Analysis of rSm16

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0-3hRP fractions and rSm16 were transferred after SDS-PAGE onto nitrocellulose membranes using an iBlot® Transfer Stack (Life Technologies). The membranes were then processed using the SnapID® system (Millipore) blocked with PBS containing 1% BSA, incubated first with rabbit anti-rSm16 antibody (1:5000) (gift from Dr Martin Gullberg, Umeå University, Sweden) for 10 min, and then goat anti rabbit antibody (1:30000) conjugated to horseradish peroxidase (Abcam). SuperSignal® West Pico chemiluminescence reagent (Thermo Scientific) was used to reveal labelled proteins using X-ray film imaging (GE Healthcare).

Sanin D.E, & Mountford A.P. (2015). Sm16, a major component of Schistosoma mansoni cercarial excretory/secretory products, prevents macrophage classical activation and delays antigen processing. Parasites & Vectors, 8, 1.

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Evaluating TGF-β1/Smad Signaling in Lung Tissue

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Activation of the TGF-β1/Smad signaling pathway was assessed in the present study using western blot analysis. The pre-cleaned lung tissue was homogenized in RIPA buffer with PMSF. Following centrifugation at 14,000 × g at 4°C, the supernatants were used for western blot analysis. The protein concentration was determined using a BCA protein assay kit (Santa Cruz Biotechnology, Inc., Dallas, TX, USA). The proteins (50 µg) were then separated by SDS PAGE (4% stacking gel and 10% separation gel) vertically and semi-dry transferred onto polyvinylidene fluoride membranes. Antibodies against TGF-β1 (ab64715; Abcam), Smad3 (A27034; Cell Signaling Technology, Inc., Danvers, MA, USA), acetylated (Ac)-Smad3 (#9513; Cell Signaling Technology, Inc,), Sirt1 (#8469; Cell Signaling Technology, Inc.), α-SMA (Abcam), collagen I (Abcam) and GAPDH (#MA1-16757; Invitrogen; Thermo Fisher Scientific, Inc.) were used to incubate the membranes. Rabbit anti-mouse (sc-358943), bovine anti-goat (sc-2384) and bovine anti-rabbit (sc-2385) secondary antibodies conjugated to horseradish peroxidase (Santa Cruz Biotechnology, Inc.) were used to incubate the membranes. Subsequently, Super Signal West Pico chemiluminescence reagent (Thermo Fisher Scientific, Inc.) was used to develop the membranes and the immunoblots were visualized on X-ray films.

Yang T., Wang J., Pang Y., Dang X., Ren H., Liu Y., Chen M, & Shang D. (2016). Emodin suppresses silica-induced lung fibrosis by promoting Sirt1 signaling via direct contact. Molecular Medicine Reports, 14(5), 4643-4649.

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Western Blot Analysis of Cell Lysates

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After SNG treatment, Western blot analysis was performed as described previously [15 (link)]. The cells were washed twice with PBS and were lysed in a RIPA lysis buffer (50 mM Tris HCl pH 7.4, 1% NP-40, 40 mM NaF, 10 mM NaCl, 10 mM Na3VO4, 1 mM phenyl methyl sufonyl fluoride, 10 mM dithiothreitol, and EDTA-free protease inhibitor tablet). The cell lysates were centrifuged and the total protein was determined using a Bio-Rad protein assay. The lysates were mixed with a 6x loading buffer and boiled at 100 °C for 3 min. Samples at 30–50 μg/lane were resolved using SDS-PAGE and the separated proteins were transferred on to a nitrocellulose membrane by a wet transfer method using Bio-Rad electro transfer apparatus. Following the transfer, the blots were blocked with 5% non-fat milk in Tris-buffer saline containing 0.1% Tween-20. The blots were then incubated with primary antibodies followed by a secondary antibody. The protein bands were visualized using a Super Signal West Pico Chemiluminescence reagent (Thermo Scientific, Pleasanton, CA, USA).

Alakkal A., Thayyullathil F., Pallichankandy S., Subburayan K., Cheratta A.R, & Galadari S. (2022). Sanguinarine Induces H2O2-Dependent Apoptosis and Ferroptosis in Human Cervical Cancer. Biomedicines, 10(8), 1795.

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Western Blot Protein Analysis Protocol

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For Western blots, lysates were normalized for total protein content using Protein Assay Dye Reagent (Bio-Rad). The samples were prepared by adding 1× of the final concentration of NuPAGE LDS Sample Buffer (Invitrogen), followed by incubation at 95 °C for 5 min. Subsequently, the protein samples were resolved on a mini NuPAGE 4–12% Bis-Tris gel (Thermo Fisher, Scientific, Waltham, MA, USA) in the presence of a 1× NuPAGE MES SDS running buffer (Thermo Fisher, Scientific, Waltham, MA, USA). The proteins were then transferred to Immobilon-FL (Millipore). The membranes were blocked for 1 h at room temperature with 5% BSA in TBS, followed by incubation with the indicated primary antibodies. Horse peroxidase-conjugated secondary antibodies were used for detection with SuperSignal West Pico chemiluminescence reagent (Thermo Fisher, Scientific, Waltham, MA, USA). The detection of CBS was performed using commercial antibodies from Santa Cruz.

Paul B.D., Sbodio J.I, & Snyder S.H. (2022). Mutant Huntingtin Derails Cysteine Metabolism in Huntington’s Disease at Both Transcriptional and Post-Translational Levels. Antioxidants, 11(8), 1470.

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Protein Analysis Protocol for AMPK Signaling

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Protein analysis was performed as described previously (35 (link), 36 (link)). In brief, tissue was lysed in 50 mM Tris (pH 7.4), 150 mM NaCl, 1% Triton X-100, 15% glycerol, Phosphatase Inhibitor Mixtures 2 and 3 (Sigma-Aldrich), and Protease Inhibitor Mixtures 1 and 2 (Roche). Equal amounts of protein were run on NuPage 4–12% Bis-Tris gels (Invitrogen). Following SDS/PAGE and blocking, membranes were incubated overnight at 4 °C with one of the following antibodies: AMPK, phospho-AMPKα, ACC, phospho-ACC, or GAPDH (Cell Signaling Technology). Anti-rabbit Ig horseradish peroxidase-conjugated secondary antibody (Jackson ImmunoResearch Laboratories) and SuperSignal West Pico chemiluminescence reagent (Thermo Fisher Scientific) were used for detection. Protein quantification was performed using ImageJ software according to the provided protocol. Densities were calculated for each sample and analyzed across conditions.

Brynildsen J.K., Lee B.G., Perron I.J., Jin S., Kim S.F, & Blendy J.A. (2018). Activation of AMPK by metformin improves withdrawal signs precipitated by nicotine withdrawal. Proceedings of the National Academy of Sciences of the United States of America, 115(16), 4282-4287.

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Quantifying Borrelia Protein Expression

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Bacterial protein contents were assessed by electrophoresis in SDS-PAGE and staining with Coomassie brilliant blue.
For immunoblot analyses, equal loading of B. burgdorferi cell extracts was assessed by immunoblot against the constitutively-expressed FlaB subunit of the flagella, using monoclonal antibody H9724 [39 (link)]. Rabbit polyclonal antisera directed against CdaA was obtained from NeoBioLab (Woburn, MA), who used as antigen a polypeptide consisting of CdaA residues 193–205, NVDSISKAFGTRH, using their standard protocol. Bound antibodies were detected using appropriate horseradish peroxidase-conjugated secondary antibodies and SuperSignal West Pico chemiluminescence reagent (Thermo Scientific).

Savage C.R., Arnold W.K., Gjevre-Nail A., Koestler B.J., Bruger E.L., Barker J.R., Waters C.M, & Stevenson B. (2015). Intracellular Concentrations of Borrelia burgdorferi Cyclic Di-AMP Are Not Changed by Altered Expression of the CdaA Synthase. PLoS ONE, 10(4), e0125440.

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Immunoprecipitation and Immunoblotting Protocol

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For immunoprecipitation, the brain lysate was incubated with the primary antibody and protein G-conjugated Sepharose (GE Healthcare, Little Chalfont, Buckinghamshire, UK) for 2 h at 4 °C. The beads were recovered by centrifugation (400 × g for 2 min) and washed three times with Tris-buffered saline containing 0.1% Triton X-100. The beads were boiled in Laemmli sample buffer, and eluted proteins were subjected to sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE). For immunoblotting, solubilized proteins were separated by SDS-PAGE on a 10% polyacrylamide gel and transferred onto nitrocellulose membranes. After blocking with 5% nonfat dry milk in PBS containing 0.05% Tween 20, membranes were incubated with primary antibodies, followed by the incubation with HRP-conjugated secondary antibodies. Protein bands were detected using the Super Signal West Pico chemiluminescence reagent (Thermo Fisher Scientific, Waltham, MA) and a LAS-3000 Luminoimage Analyzer (Fujifilm, Tokyo, Japan).

Nakagawa N., Yagi H., Kato K., Takematsu H, & Oka S. (2015). Ectopic clustering of Cajal–Retzius and subplate cells is an initial pathological feature in Pomgnt2-knockout mice, a model of dystroglycanopathy. Scientific Reports, 5, 11163.

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Western Blot Analysis of Protein Expression

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Cells were washed twice with PBS and lysed in a RIPA lysis buffer (50 mM Tris–HCl pH 7.4, 1% NP-40, 40 mM NaF, 10 mM NaCl, 10 mM Na₃VO₄, 1 mM PMSF, 10 mM DTT, and EDTA-free protease inhibitor tablet). The cell lysates were centrifuged and total protein were determined by Bio-Rad protein assay. Lysates were mixed with 6× loading buffer and boiled at 100 °C for 3 min. Samples at 30–50 μg/lane were resolved by SDS–PAGE and the separated proteins were transferred on to nitrocellulose membrane by wet transfer method using Bio-Rad electro transfer apparatus. Following the transfer, blots were blocked with 5% non-fat milk in Tris-buffer saline containing 0.1% Tween-20. Blots were then incubated with primary antibodies followed by secondary antibody. Protein bands were visualized using Super Signal West Pico Chemiluminescence reagent (Thermo Scientific, CA, USA). Densitometry analyses were performed by normalizing target protein bands to their respective loading control using Image Studio Lite software (LI-COR Biosciences).

Thayyullathil F., Cheratta A.R., Alakkal A., Subburayan K., Pallichankandy S., Hannun Y.A, & Galadari S. (2021). Acid sphingomyelinase-dependent autophagic degradation of GPX4 is critical for the execution of ferroptosis. Cell Death & Disease, 12(1), 26.

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Immunoblot Analysis Protocol

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Immunoblot analysis was performed essentially as described [80 (link)]. Briefly, equal amounts of whole cell or tissue lysates were resolved by SDS-PAGE and electrotransferred to nitrocellulose membranes. Membranes were blocked with 10% non-fat dried milk in phosphate buffered saline containing 0.1% Tween-20 (PBS-T), rinsed with PBS-T, and incubated with protein-specific primary antibodies (1:1000 dilution) overnight at 4°C. After washing, membranes were incubated with species-specific HRP-conjugated secondary antibodies, and proteins were visualized following incubation with SuperSignal WestPico chemiluminescence reagent (Thermo Fisher Scientific, Rockford, IL) and exposure of membranes to X-ray film.

Yang W., Ramachandran A., You S., Jeong H., Morley S., Mulone M.D., Logvinenko T., Kim J., Hwang D., Freeman M.R, & Adam R.M. (2014). Integration of proteomic and transcriptomic profiles identifies a novel PDGF-MYC network in human smooth muscle cells. Cell Communication and Signaling : CCS, 12, 44.

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