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Western blot workflow. The western blot (sometimes called the protein immunoblot), or western blotting, is a widely used analytical technique in molecular biology and immunogenetics to detect specific proteins in a sample of tissue homogenate or extract. [1]
Normalization of Western blot data is an analytical step that is performed to compare the relative abundance of a specific protein across the lanes of a blot or gel under diverse experimental treatments, or across tissues or developmental stages.
A review on western blotting from 2006 describes Towbin as the author for W.blotting and Stark for Northern -- maxhebditch 14:10, 07/01/13 —Preceding undated comment added 14:12, 7 January 2013 (UTC) [ reply ]
A western blot is used for the detection of specific proteins in complex samples. Proteins are first separated by size using electrophoresis before being transferred to an appropriate blotting matrix (usually polyvinylidene fluoride or nitrocellulose ) and subsequent detection with antibodies.
Southwestern blotting was first described by Brian Bowen, Jay Steinberg, U.K. Laemmli, and Harold Weintraub in 1979. [2] During the time the technique was originally called "protein blotting". While there were existing techniques for purification of proteins associated with DNA, they often had to be used together to yield desired results.
The sample is detected on a western blot. By using electrophoretic mobility shift assay (EMSA), [ 88 ] the activation profile of transcription factors can be detected. A multiplex approach for activation profiling is a TF chip system where several different transcription factors can be detected in parallel.
The far-western blot, or far-western blotting, is a molecular biological method based on the technique of western blot to detect protein-protein interaction in vitro. [1] [2] Whereas western blot uses an antibody probe to detect a protein of interest, far-western blot uses a non-antibody probe which can bind the protein of interest.
Immunoprecipitation of intact protein complexes (i.e. antigen along with any proteins or ligands that are bound to it) is known as co-immunoprecipitation (Co-IP). Co-IP works by selecting an antibody that targets a known protein that is believed to be a member of a larger complex of proteins.