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Western blotting is a technique that uses specific antibodies to identify proteins that have been separated based on size by gel electrophoresis. The immunoassay uses a membrane made of nitrocellulose or PVDF (polyvinylidene fluoride).
General Protocol for Western Blotting Protein separation by gel electrophoresis 1. Load equal amounts of protein (20 μg) into the wells of a mini (8.6 x 6.7 cm) or midi (13.3 x 8.7 cm) format SDS-PAGE gel, along with molecular weight markers. 2. Run the gel for 5 min at 50 V. 3. Increase the voltage to 100–150 V to finish the run in about 1 hr.
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Here, you can find a collection of western blot recipes for commonly used protein electrophoresis and western blot buffers and stock solutions, and general western blotting protocols for chemiluminescent and fluorescent detection to guide you through your experiment.
Western blot is a technique that is very useful for protein detection as it allows the user to quantify the protein expression as well. This paper covered the protocol, the theory behind that protocol, and some troubleshooting techniques.
- Tahrin Mahmood, Ping-Chang Yang
- 10.4103/1947-2714.100998
- 2012
- N Am J Med Sci. 2012 Sep; 4(9): 429-434.
Western blot guide. Find out the difference between indirect and direct labeling in western blot and learn different methods of immunoblot detection. Recipes for western blot buffers and stock solutions.
Western blotting is a technique that uses specific antibodies to identify proteins separated by size through gel electrophoresis. The immunoassay uses a membrane made of nitrocellulose or PVDF (polyvinylidene fluoride). The gel is placed next to the membrane, and an electrical current is applied.
