Total cellular proteins and nuclear proteins were separately extracted using the Total Protein Isolation Kit (Sangon Company, China) and Nuclear Protein Isolation Kit (Sangon Company). Proteins were quantified by Bicinchoninic acid assay kit (Sangon Company). The protein samples were loaded on SDS–PAGE gels and electrophoresed under standard conditions. Western blotting was performed using nitrocellulose membranes. After blocking, membranes were incubated with primary antibodies (1:200–1:500) at 4 °C overnight. After rinsing, incubation was conducted with secondary horseradish peroxidase-conjugated goat anti-rabbit or mouse IgG antibody (Bioss Biotechnology, China) and exposed to film. Primary antibodies included anti-Frizzled (FZD, Immunoway, Catalog: YT1783, USA), anti-phospho-Frizzled (p-FZD, Immunoway, Catalog: YP0173), anti-β-Catenin (Boster Biotechnology, Catalog: BM1575, China), anti-Oct4 (Santa Cruz Biotechnology, Catalog: sc-5279, USA), anti-Sox2 (Santa Cruz Biotechnology, Catalog: sc-17320), anti-βIII-Tubulin (Santa Cruz Biotechnology, Catalog: sc-58888), anti-Map2 (Santa Cruz Biotechnology, Catalog: sc-20172), anti-Nestin (Santa Cruz Biotechnology, Catalog: sc-20978), and anti-Gapdh (Cell Signaling Technology, Catalog: #2118, USA).
Anti β catenin
Manufactured by Boster Bio
Sourced in China
Anti-β-Catenin is a primary antibody that specifically binds to the β-Catenin protein, a key component of the Wnt signaling pathway. It can be used in various laboratory techniques, such as Western blotting, immunohistochemistry, and immunocytochemistry, to detect and quantify the expression of β-Catenin in biological samples.
Automatically generated - may contain errors
Lab products found in correlation
Anti gapdh, by Boster Bio (2 mentions)
Anti map2, by Santa Cruz Biotechnology (1 mentions)
Anti nestin, by Santa Cruz Biotechnology (1 mentions)
Anti sox2, by Santa Cruz Biotechnology (1 mentions)
Anti oct4, by Santa Cruz Biotechnology (1 mentions)
Anti gapdh, by Cell Signaling Technology (1 mentions)
Bicinchoninic acid assay kit, by Sangon (1 mentions)
Chemiluminescence kit, by Vazyme (1 mentions)
Anti akt, by Cell Signaling Technology (1 mentions)
Anti ki67, by Proteintech (1 mentions)
Anti β tubulin, by Boster Bio (1 mentions)
Cell cycle assay kit, by Dojindo Laboratories (1 mentions)
Anti phospho akt, by Cell Signaling Technology (1 mentions)
Anti cdk2, by ABclonal (1 mentions)
Anti cdk4, by ABclonal (1 mentions)
Anti gsk3β, by Boster Bio (1 mentions)
Anti cyclin d1, by Abcam (1 mentions)
Anti bcl 2, by Abcam (1 mentions)
Acetonitrile, by Sinopharm (1 mentions)
Ethanol, by Sinopharm (1 mentions)
5 protocols using anti β catenin
1
Protein Expression Analysis of Neural Stem Cells
2
Combinatorial Therapeutic Assessment with MK-2206 and Finasteride
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MK-2206 2HCl and finasteride (Fin) were purchased from Shanghai Selleck Chemicals Co., Ltd. Shanghai, China. Organic reagents such as ethanol and acetonitrile were obtained from Sinopharm Chemical Reagent Co. Ltd. Shanghai, China. Cell Cycle Assay Kit was acquired from Dojindo, Kumamoto, Japan. Primary antibodies included anti-β-Catenin, anti-GSK3β, anti-phospho-GSK3β, anti-GAPDH, and anti-β-tubulin (Boster Biological Technology, Pleasanton, CA, United States), anti-Bcl2, anti-Bax, and anti-Cyclin D1 (Abcam plc, Cambridge, United Kingdom), anti-Akt and anti-phospho-Akt (Cell Signaling Technology, Danvers, MA, United Ststes), anti-Wnt10b, anti-CDK2, anti-CDK4, and anti-P21 (ABclonal, Wuhan, China), and anti-ki67 (Proteintech, Wuhan, China). The chemiluminescence kit was obtained from Vazyme Biotech, Nanjing, China. The terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) detection kit was acquired from Promega Corporation, Madison, WI, United States.
3
Western Blot Analysis of Brain Tissue Proteins
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Cells or samples of brain tissue were lysed with radioimmunoprecipitation assay buffer on ice for 30 min. Next, a 30 μg sample of total protein from each lysate was subjected to 10% sodium dodecyl sulphate‐polyacrylamide gel electrophoresis, and the separated protein bands were transferred onto 0.2‐μm polyvinylidene difluoride membranes that were subsequently blocked with 5% nonfat milk for 1 h. Next, the membranes were incubated with anti‐claudin‐5 (Beyotime; CAT. No. PB0123, 1:800), anti‐Wnt3a (Boster; CAT. No. BA2628‐2, 1:1000), anti‐β‐catenin (Boster; CAT. No. BA0426, 1:1000), anti‐B1R (Abcam; CAT. No. ab77366, 1:100), anti‐Occludin (Boster; CAT. No. BM4832, 1:1000), and anti‐glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH; Abcam; CAT. No. ab8245, 1:3000) antibodies overnight at 4°C; after which, they were washed three times with TBST and incubated for 1 h with an HRP‐conjugated secondary antibody at room temperature. The signals were detected with enhanced chemiluminescence reagents. The gray level of each blot band was recorded using ImageJ software (Wayne Rasband Company; Ver. 1.48). GAPDH served as an internal reference standard when calculating relative levels of protein expression.
4
Cellular Protein Quantification and Analysis
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Cells were cleaved on ice for 30 min by protein lysate (RIPA) (Beyotime, Shanghai, China) supplemented with a protease inhibitor (Pierce, Rockford, IL, USA). After centrifugation at 12,000 rpm for 10 min in a 4 °C centrifuge, the supernatant was aspirated into a 1.5 mL centrifuge tube. The total cellular protein was separated by 10% SDS–polyacrylamide gel and then transferred to a PVDF membrane (Millipore, Boston, MA, USA). Next, the membrane was sealed with 5% skim milk powder for 2 h. After this, the membrane was incubated with primary antibody overnight at 4 °C, followed by incubation of the secondary antibody for 1 h at room temperature. Protein bands were presented using chemiluminescence solutions and quantified using Image Lab and Document Image processing. Anti-PPARγ from Abcam (Cambridge, UK); anti-aP2, anti-Adiponectin, anti-Cyclin B, anti-Cyclin D, anti-Cyclin E, and anti-CDK4 from Santa Cruz (Dallas, TX, USA); and anti-β-actin and anti-β-catenin from Boster (Wuhan, China) were used.
5
Protein Expression Analysis in Lung Cancer Cells
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Radioimmunoprecipitation (RIPA) lysis buffer (Beyotime) was used to extract total protein from A549 and H1299 cells. The same amount protein was subjected to sodium dodecyl‐sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) gel and then transferred onto a polyvinylidene fluoride (PVDF) membrane (Beyotime). The membrane was blocked with 5% skimmed milk and incubated with primary antibodies including anti‐NOVA2 (1:2000, Boster), anti‐β‐catenin (1:1500, Boster), anti‐c‐Myc (1:2000, Boster), anti‐CyclinD1 (1:1000, Boster), or anti‐GAPDH (1:2000, Boster). After the membrane was hatched with secondary antibody (1:10,000, Boster), the protein blots were visualized by Ultra Sensitive ECL Chemiluminescence Substrate (Boster). The relative protein expression was analyzed using ImageJ software (National Institutes of Health).
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