Pierce ecl western blotting solution

Manufactured by Thermo Fisher Scientific

Sourced in United States

The Pierce ECL Western Blotting Solution is a chemiluminescent substrate used for the detection of proteins in western blotting experiments. It is designed to produce a luminescent signal when exposed to horseradish peroxidase (HRP)-labeled secondary antibodies.

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Pierce ECL (169 citations) ECL solution (151 citations) Pierce ECL solution (14 citations) Pierce ECL Western Blotting Substrate solution (3 citations)

5 protocols using pierce ecl western blotting solution

Western Blot Analysis of Trout Mucosal pIgR

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Ten μl of each trout mucus pool sample were mixed with 10 μl of Laemlli sample buffer (Bio-Rad) and were separated using 4–15% Mini-PROTEAN^® TGX™ precast gels (Bio-Rad) under non-reducing conditions and transferred onto PVDF membranes (Thermo Scientific). Membranes were blocked overnight in 5% non-fat milk (LabScientific) and then incubated for 1 h with primary antibody (1:1000 rabbit anti-trout pIgR), followed by 45 min with secondary antibody (1:2500 horseradish peroxidase-conjugated donkey anti-rabbit IgG, Jackson Immunoresearch). Membranes incubated with rabbit prebleed antibody were used as a negative control. After three washes, membranes were developed using Pierce^® ECL western blotting solution and exposed in darkroom to CL-X Posure™ film (Thermo) or scanned using Bio-Rad ChemiDoc™ XRS + with Image Lab™ Software.

Kelly C., Takizawa F., Sunyer J.O, & Salinas I. (2017). Rainbow trout (Oncorhynchus mykiss) secretory component binds to commensal bacteria and pathogens. Scientific Reports, 7, 41753.

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Quantifying Plasma Protein Biomarkers

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Plasma was separated from EDTA whole blood by centrifugation at 2000G for 15 minutes at 4°C. A 1:50 dilution was prepared using SDS-PAGE loading buffer. Proteins were separated by SDS-PAGE and transferred to nitrocellulose membranes for immunoblotting. Membranes were probed with polyclonal primary antibodies: rabbit anti-CSF1 (1:500, MyBioSource, MBS551037) and 1:2000 sheep anti-Transferrin (1:2000, Abcam, ab9033) in PBS/3% milk powder/0.1 % (v/v) Tween20 at 4°C overnight. The secondary antibodies used were goat anti-rabbit HRP (1:5000, Cell Signalling Technologies, #7074) and rabbit anti-sheep HRP (1:10,000, Abcam, ab97130). Blots were visualised using Pierce™ ECL western blotting solution (Thermo Fisher Scientific).

Pridans C., Raper A., Davis G.M., Alves J., Sauter K.A., Lefevre L., Regan T., Meek S., Sutherland L., Thomson A.J., Clohisey S., Bush S.J., Rojo R., Lisowski Z.M., Wallace R., Grabert K., Upton K.R., Tsai Y.T., Brown D., Smith L.B., Summers K.M., Mabbott N.A., Piccardo P., Cheeseman M.T., Burdon T, & Hume D.A. (2018). Pleiotropic Impacts of Macrophage and Microglial Deficiency on Development in Rats with Targeted Mutation of the Csf1r Locus. The Journal of Immunology Author Choice, 201(9), 2683-2699.

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Apoptosis Pathway Protein Analysis by Western Blot

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Western blot was performed as described previously [30 (link)]. Antibody concentrations of primary antibodies were used as follows: Anti-DR4 (1:1000; Pro Sci, Fort Collins, CO, USA), anti-caspase-8 (1:1000; Enzo), anti-CDK9, anti-PARP, anti-FADD, anti-Bax, anti-Bak, anti-Mcl-1, anti-Bcl-xL, anti-Bcl-2, anti-cFLIP (AdipoGen, San Diego, CA, USA), anti-cIAP1, anti-cIAP2, anti-XIAP, anti-survivin (1:1000; Cell Signaling Technology), anti-caspase-9 (1:500; Cell Signaling Technology), anti-DR5, anti-Bid (1:2000; Cell Signaling Technology), anti-β-actin (1:5000; Sigma-Aldrich), anti-caspase-3 (1:2000; R&D, Minneapolis, MN, USA), anti-RNA polymerase II total (RNA Pol II) (1:2000), anti-pSer2 RNA Pol II (1:5000; Covance, Princeton, NJ, USA). Immuno-complexes were detected using peroxidase-conjugated anti-mouse IgG, anti-rabbit IgG, and anti-goat IgG (1:5000; Cell Signaling Technology) followed by chemiluminescence detection (Pierce ECL Western Blotting Solution; Thermo Fisher Scientific).

Shen X., Kretz A.L., Schneider S., Knippschild U., Henne-Bruns D., Kornmann M., Lemke J, & Traub B. (2023). Evaluation of CDK9 Inhibition by Dinaciclib in Combination with Apoptosis Modulating izTRAIL for the Treatment of Colorectal Cancer. Biomedicines, 11(3), 928.

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Quantification of CSF1 and Transferrin in Plasma

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Plasma was separated from EDTA whole blood by centrifugation at 2000 G for 15 min at 4°C. A 1:50 dilution was prepared using SDS-PAGE loading buffer. Proteins were separated by SDS-PAGE and transferred to nitrocellulose membranes for immunoblotting. Membranes were probed with polyclonal primary Abs: rabbit anti-CSF1 (1:500, MBS551037; MyBioSource) and 1:2000 sheep anti-Transferrin (1:2000, ab9033; Abcam) in PBS/3% milk powder/0.1% (v/v) Tween 20 at 4°C overnight. The secondary Abs used were goat anti-rabbit HRP (1:5000, no. 7074; Cell Signaling Technologies) and rabbit anti-sheep HRP (1:10,000, ab97130; Abcam). Blots were visualized using Pierce ECL Western blotting solution (Thermo Fisher Scientific).

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Western Blot Analysis of Cell Signaling

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Cells were lysed in lysis buffer (30 mM Tris-HCl, pH 7.4; 150 mM NaCl; 2 mM EDTA; 2 mM KCl; 10% glycerol; 1% Triton X-100; Protease Inhibitor Tablet (Pierce™, Thermo Fisher Scientific), Phosphatase Inhibitor Cocktail 2 (Sigma-Aldrich, St. Louis, MO, USA)). Proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to a nitrocellulose membrane. Anti-CDK9, anti-Cyclin T1, anti-Bid, anti-Bax, anti-Bak, anti-Bcl-xL, anti-Mcl-1, anti-cIAP1, anti-Survivin, anti-XIAP, anti-PARP, anticleaved PARP (1:1000; Cell Signaling Technology), antiactin (1:10,000; Sigma-Aldrich), anti-RNA polymerase II total (1:2000), anti-RNA polymerase II pSer2 (1:5000), and anti-RNA polymerase II pSer5 (1:1000; Covance, Princeton, NJ, USA) were used as primary antibodies. Immunocomplexes were detected using peroxidase-conjugated anti-mouse IgM (1:10,000; SouthernBiotech, Birmingham, AL, USA), anti-mouse IgG (1:10,000), and anti-rabbit IgG (1:5000) (both purchased from Cell Signaling Technology) followed by chemiluminescence detection (Pierce ECL Western Blotting Solution; Thermo Fisher Scientific).

Kretz A.L., Schaum M., Richter J., Kitzig E.F., Engler C.C., Leithäuser F., Henne-Bruns D., Knippschild U, & Lemke J. (2017). CDK9 is a prognostic marker and therapeutic target in pancreatic cancer. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine, 39(2).

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