Western blotting stripping buffer

Manufactured by Thermo Fisher Scientific

Sourced in United States

Thermo Fisher Scientific's Western blotting stripping buffer is a solution designed to remove primary and secondary antibodies from Western blot membranes. This allows the membrane to be reprobed with different antibodies, enabling multiple analyses to be performed on a single sample.

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Lab products found in correlation

Ripa lysis buffer, by Merck Group (1 mentions) Ecl detection reagent, by Merck Group (1 mentions) Mouse anti glyceraldehyde 3 phosphate dehydrogenase gapdh antibody, by Beyotime (1 mentions) Chemidoc touch imaging system, by Bio-Rad (1 mentions) Anti p53, by Santa Cruz Biotechnology (1 mentions) Enhanced chemiluminescence, by Thermo Fisher Scientific (1 mentions) Anti α sma antibody, by Cell Signaling Technology (1 mentions) Anti rabbit igg secondary antibody, by Santa Cruz Biotechnology (1 mentions) Anti gapdh antibody, by Cell Signaling Technology (1 mentions) Chemidoc imaging system, by Bio-Rad (1 mentions)

Spelling variants of this product

Stripping buffer (117 citations) Restore Western Blotting Stripping Buffer (9 citations) Restore Plus Western Blotting Stripping Buffer (6 citations)

2 protocols using western blotting stripping buffer

Quantifying Acetylated p53 in Hippocampus

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Western blotting was conducted to semiquantify the levels of acetylated p53 and p53 in the hippocampus at 24–25 h after SE. The hippocampal tissues were homogenised, and the total proteins were extracted using RIPA lysis buffer (Sigma) including a protease inhibitor and a phosphorylase inhibitor (Roche, USA). The Western blots were incubated with rabbit anti-acetylated p53-K120 antibody (1:5000; Abcam, USA) and mouse anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibody(1:2000; Beyotime Biotechnology, China) overnight at 4 °C. After the detection of acetylated p53 bands and GAPDH bands by using ECL detection reagents (Millipore, USA), the blots were washed in Western blotting stripping buffer (Thermo, USA) for 10 min at room temperature and incubated with anti-p53 (1:250; Santacruz, USA) for 2 h at room temperature. Western blot images were captured using ChemiDoc^TM Touch Imaging System (Bio-Rad). Acetylated p53 and total p53 levels were quantified through densitometry by using ImageJ software.

Liu J., Yang B., Zhou P., Kong Y., Hu W., Zhu G., Ying W., Li W., Wang Y, & Li S. (2017). Nicotinamide adenine dinucleotide suppresses epileptogenesis at an early stage. Scientific Reports, 7, 7321.

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TGFβ-1 and C53 Effects on Myofibroblast Markers

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HCFs and HRFs were cultured in 6-well plates and starved for 48 hours with 0.01% FBS medium after reaching 80% confluency. The cells were then treated with TGFβ−1 (5 ng/ml) alone or with C53 (10⁻⁶ M) for 24, 48 and 72 hours. Cell lysates were harvested at each indicated time point with 200uL NP-40 lysis buffer containing protease inhibitors. After 30 min of lysing, the supernatant was collected after centrifuging. Supernatant from different groups were then used for western blotting. Anti-α-SMA antibody (1:1000, Cell Signaling, Danvers, MA) and anti-rabbit IgG secondary antibody (Santa Cruz Biotechnology, Dallas, TX) were used for blotting. Western blotting stripping buffer (Thermo Fisher Scientific, Waltham, MA) was applied to remove antibodies before GAPDH blotting. GAPDH was used as loading control and anti-GAPDH antibody (Cell Signaling, Danvers, MA) and anti-rabbit IgG secondary antibody (Santa Cruz Biotechnology, Dallas, TX) were used. Enhanced chemiluminescence (Thermo Fisher Scientific, Waltham, MA) signals after blotting were read by a ChemiDoc Imaging System (Bio-Rad, Hercules, CA). Band intensity and normalization was quantified with ImageJ according to the provided instructions (NIH, Rockville, MD).

Chen Y., Zheng Y., Iyer S.R., Harders G.E., Pan S., Chen H.H., Ichiki T., Burnett JC J.r, & Sangaralingham S.J. (2019). C53: A Novel Particulate Guanylyl Cyclase B Receptor Activator That Has Sustained Activity In Vivo With Anti-Fibrotic Actions in Human Cardiac and Renal Fibroblasts. Journal of molecular and cellular cardiology, 130, 140-150.

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