The expression levels of GATA6, GATA4, RBPJ, BCL-2, Bax, and cleaved caspase-3 in spinal cord tissues were measured with Western Blotting. Total proteins were extracted from the L4-L6 segments of the spinal cords with RIPA buffer (KangChen, China). The antibodies used were rabbit polyclonal anti-GATA6 (Affinity, AF5270, China), rabbit polyclonal anti-GATA4 (Affinity, AF5245, China), rabbit polyclonal anti-RBPJ (Affinity, DF7453, China), rabbit monoclonal anti-Bax (#2772; Cell Signaling Technology, Danvers, MA, USA), rabbit polyclonal anti-Bcl-2 (26593-1-AP, ProteinTech, Rosemont, IL, USA), rabbit polyclonal anti- cleaved caspase-3 (ab2302; Abcam, Cambridge, MA, USA), rabbit anti-GAPDH (Boster, A00227, China), and HRP-conjugated secondary antibodies (Beyotime, China).
Rabbit anti gapdh
Manufactured by Boster Bio
Sourced in United States, United Kingdom, China
Rabbit anti-GAPDH is a primary antibody that specifically recognizes the GAPDH (Glyceraldehyde-3-Phosphate Dehydrogenase) protein. GAPDH is a widely expressed and highly conserved enzyme involved in glycolysis. The Rabbit anti-GAPDH antibody can be used to detect and quantify GAPDH expression in various biological samples.
Automatically generated - may contain errors
Lab products found in correlation
Hrp conjugated secondary antibody, by Beyotime (1 mentions)
Rabbit monoclonal anti bax, by Cell Signaling Technology (1 mentions)
Ab2302, by Abcam (1 mentions)
Quantity one software, by Bio-Rad (1 mentions)
Nondenaturing lysis buffer, by Applygen (1 mentions)
Pvdf membrane, by Merck Group (1 mentions)
Horseradish peroxidase hrp conjugated goat anti rabbit igg, by Beyotime (1 mentions)
Rabbit anti caspase 3, by Boster Bio (1 mentions)
3 protocols using rabbit anti gapdh
1
Spinal Cord Protein Expression Analysis
2
Uterine Protein Extraction and Western Blot Analysis
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Mice uterine proteins were extracted with non‐denaturing lysis buffer (Applygen, Beijing, China), and the protein concentration was examined using a Bicinchoninic Acid Protein Assay Kit (Pierce, Rockford, IL, USA). Uterine proteins were separated by 10% SDS‐PAGE and transferred onto a nitrocellulose membrane (Pall, New York, NY, USA). The membranes were blocked with 10% bovine serum albumin (BSA) in TBST at 37°C for 1 hr and then incubated with the primary antibodies at 4°C overnight. The following primary antibodies were used: rabbit anti‐CD49b (ab133557; Abcam, Cambridge, UK) and rabbit anti‐GAPDH (Boster, Wuhan, China). The membranes were washed and incubated with goat anti‐rabbit secondary antibody conjugated with horseradish peroxidase (HRP) (KPL, Gaithersburg, MD, USA) at 37°C for 1 hr. Then, the membranes were washed. Chemiluminescence reactions were performed with an ECL Detection Kit (Pierce), and images were acquired using Kodak X‐Omat film (Carestream, Xiamen, China). Relative protein levels were analysed using Bio‐Rad Quantity One software (Bio‐Rad, Hercules, CA, USA) and were normalized to GAPDH.
3
Neuronal Protein Isolation and Western Blot
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Neuronal proteins were isolated using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and 10% acrylamide gels (Solarbio, Beijing China). The proteins were transferred to polyvinylidene di uoride (PVDF) membranes (Millipore, Burlington, Massachusetts, USA) using electroblotting. Then the membranes with the transferred proteins were blocked in phosphate-buffered saline with 0.1% Tween (PBST) containing 10% bovine serum albumin (BSA) at room temperature for 2h. The membranes were incubated for 2h in Tris-buffered saline with 0.1% Tween (TBST) with primary antibodies, including rabbit anti-BDNF (1:800), rabbit anti-RhoA (1:1000), rabbit anti-Caspase-3 (1:1000), and rabbit anti-GAPDH (1:1000) (Boster, Wuhan, China ). After three washes for 10 min each in TBST, the membranes were incubated for 1h at 37℃ with horseradish peroxidase (HRP) conjugated goat anti-rabbit IgG and diluted at 1:800 (Beyotime, Beijing, China). Then the membranes were washed three times in TBST and processed using the enhanced chemiluminescence (ECL) detection system. An antibody to GAPDH was used as the loading control. All experiments were repeated three times. The expression level of proteins was calculated as an average of the densities per band area from each group.
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