Gapdh

Manufactured by Southern Biotech

Sourced in United States

GAPDH is a core enzyme involved in glycolysis, the process of converting glucose into energy. It catalyzes the reversible oxidation of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate. GAPDH is commonly used as a reference gene or loading control in molecular biology techniques.

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Lab products found in correlation

Enhanced chemiluminescence kit, by Cytiva (2 mentions) Protease inhibitor cocktail, by Merck Group (2 mentions) Active β catenin, by Cell Signaling Technology (1 mentions) Total β catenin, by Cell Signaling Technology (1 mentions) Cyclin b1, by Cell Signaling Technology (1 mentions) Cyclin d1, by Cell Signaling Technology (1 mentions) C myc, by Cell Signaling Technology (1 mentions) Polyvinylidene difluoride membrane, by Bio-Rad (1 mentions) Image pro plus software 6, by Media Cybernetics (1 mentions) Pi3k p85, by Santa Cruz Biotechnology (1 mentions) Histone h3, by Bioss Antibodies (1 mentions) Plcγ1, by Santa Cruz Biotechnology (1 mentions) Qproteome cell compartment kit, by Qiagen (1 mentions) β actin, by Abcepta (1 mentions) β catenin, by Santa Cruz Biotechnology (1 mentions) E cadherin, by Santa Cruz Biotechnology (1 mentions) Complete protease inhibitor cocktail tablet, by Roche (1 mentions) Bicinchoninic acid protein assay kit, by Dingguo (1 mentions) P c jun, by Cell Signaling Technology (1 mentions) C jun, by Cell Signaling Technology (1 mentions)

3 protocols using gapdh

Western Blot Analysis of PCDH17 Pathway

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At 48 h post-transfection, cells were harvested and lysed with M-PER Mammalian Protein Extraction Reagent (Pierce, Cramlington, UK) containing a protease inhibitor cocktail (Sigma-Aldrich). Proteins in cell lysates (50 μg of total protein) were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and then transferred to polyvinylidene difluoride membranes (Bio-Rad, Hercules, CA, USA). We used primary antibodies against PCDH17 (Sigma-Aldrich), active β-catenin, total β-catenin, c-Myc, cyclin D1, cyclin B1, p27, p21 (Cell Signaling Technology, USA) and GAPDH (Southern Biotech, Birmingham, AL, USA). Protein bands were visualized using an enhanced chemiluminescence kit (Amersham Pharmacia Biotech, Piscataway, NJ, USA).

Yin X., Xiang T., Mu J., Mao H., Li L., Huang X., Li C., Feng Y., Luo X., Wei Y., Peng W., Ren G, & Tao Q. (2016). Protocadherin 17 functions as a tumor suppressor suppressing Wnt/β-catenin signaling and cell metastasis and is frequently methylated in breast cancer. Oncotarget, 7(32), 51720-51732.

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Cell Lysate Extraction and Protein Analysis

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Total cell lysates were isolated by radioimmunoprecipitaion assay (RIPA) lysis buffer (50 mM HEPES, pH 7.4, 150 mM NaCl, 1 mM EDTA, 1% Triton X-100, 0.1% SDS) containing 1% PMSF and Complete Protease Inhibitor Cocktail tablets (Roche, Indianapolis, IN). Plasma membrane and nuclear lysates were extracted using the Qproteome Cell Compartment Kit (Qiagen, Leipzig, Germany). Protein concentrations were determined by a bicinchoninic acid protein assay kit (Beijing Dingguo Changsheng Biotechnology, Beijing, China). Equal amounts of protein were used for Western blot analysis with appropriate antibodies against p120, PLC-γ1, E-cadherin, β-catenin, integrin α2 (plasma membrane marker), PI3K p85, or nucleolin (Santa Cruz), PIKE or PKC-ζ (Millipore, Billerica, MA), phosphorylated nucleolin (p-nucleolin, Abcam, Cambridge, MA), histone H3 (nuclear marker, Bioss, Beijing, China), GAPDH (Southern Biotechnology Associates, Birmingham, AL), or β-actin (Abgent, San Diego, CA). Quantifications of proteins within the bands of interest were performed using Image-pro plus software 6.0 (Media Cybernetics). Each experiment was repeated 3 times.

Li L., Ji S., Shrestha C., Jiang Y., Liao L., Xu F., Liu Z., Bikle D.D, & Xie Z. (2020). p120-catenin suppresses proliferation and tumor growth of oral squamous cell carcinoma via inhibiting nuclear phospholipase C-γ1 signaling. Journal of cellular physiology, 235(12), 9399-9413.

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Western Blot Analysis of Apoptosis Markers

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Forty-eight hours after transfection, cells were harvested and lysed in M-PER Mammalian Protein Extraction Reagent (Pierce, Thermo Scientific, Cramlington, UK) containing a protease inhibitor cocktail (Sigma Aldrich, St. Louis, MO). A total of 50 µg of protein lysates were separated by sodium dodecyl sulphate/polyacrylamide gel electrophoresis (SDS-PAGE) and then transferred onto a PVDF membrane (Bio-Rad, Hercules, CA, USA). The primary antibodies were used: c-Jun (#9165, cell signaling Technology, Danvers, MA), p-c-Jun (#2361, cell signaling),cleaved caspase-3 (#9661, Cell Signaling), p53 (sc-126, Santa Cruz, CA), BAX (#9942, cell signaling), and GAPDH (Southern Biotech,Birmingham, USA) was used as a control. Proteins were visualized using an enhanced chemiluminescence kit (Amersham Pharmacia Biotech, Piscataway, NJ, USA).

Xiao Y., Xiang T., Luo X., Li C., Li Q., Peng W., Li L., Li S., Wang Z., Tang L., Ren G, & Tao Q. (2014). Zinc-Finger Protein 545 Inhibits Cell Proliferation as a Tumor Suppressor through Inducing Apoptosis and is Disrupted by Promoter Methylation in Breast Cancer. PLoS ONE, 9(10), e110990.

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