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Western blot HIV test where the first two strips are negative and positive controls followed by actual tests. The western blot is extensively used in biochemistry for the qualitative detection of single proteins and protein-modifications (such as post-translational modifications).
The detection of horseradish peroxidase by enzymatic chemiluminescence (ECL) is a common method of detecting antibodies in western blotting. Another example is the enzyme luciferase, this is found in fireflies and naturally produces light from its substrate luciferin.
Immunochemical techniques include: enzyme-linked immunosorbent assay, immunoblotting (e.g., Western blot assay), precipitation and agglutination reactions, immunoelectrophoresis, immunophenotyping, immunochromatographic assay and cyflometry. One of the earliest examples of immunochemistry is the Wasserman test to detect syphilis.
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.
As an analytical biochemistry assay and a "wet lab" technique, ELISA involves detection of an analyte (i.e., the specific substance whose presence is being quantitatively or qualitatively analyzed) in a liquid sample by a method that continues to use liquid reagents during the analysis (i.e., controlled sequence of biochemical reactions that will generate a signal which can be easily ...
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.
Micrograph of a GFAP immunostained section of a brain tumour.. In biochemistry, immunostaining is any use of an antibody-based method to detect a specific protein in a sample. . The term "immunostaining" was originally used to refer to the immunohistochemical staining of tissue sections, as first described by Albert Coons in 1941.
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.
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