Western blot

Western blot is a laboratory method for detecting a specific protein in a sample. It separates proteins by size, transfers them to a membrane, and detects the target with antibodies.

SDS-PAGE: A gel electrophoresis method that separates denatured proteins mainly by molecular mass. It separates the sample’s proteins before transfer to the membrane.
Protein: A molecule made of one or more chains of amino acids folded into functional structures. Western blots separate and detect proteins rather than genes or metabolites.
Protein expression: The production of a protein from its encoding genetic information. Blots compare protein abundance across tissues, treatments, or experimental conditions.
ELISA: An antibody-based assay that uses an enzyme-linked signal to detect or quantify a target in a sample. ELISA quantifies targets in wells without separating proteins into visible bands.
Edwin Southern: A British molecular biologist who developed the DNA-detection method called Southern blotting. His earlier technique inspired the name and general format of Western blotting.
Electrophoretic transfer: The movement of molecules from a gel onto a membrane under an electric field. It moves separated proteins from the gel onto the blotting membrane.
Protein denaturation: The disruption of a protein’s native structure without necessarily breaking its peptide bonds. Denaturation prepares proteins for size-based separation and affects which epitopes remain detectable.
Phosphorylation: The addition of a phosphate group to a molecule, often a protein, by an enzyme. Phospho-specific antibodies let blots detect particular protein modification states.
Immunohistochemistry: A tissue-staining method that uses antibodies to reveal the location of specific molecules. It preserves spatial context that a bulk protein blot loses.
W. Neal Burnette: A researcher credited with naming Western blotting in a 1981 publication. His paper established the technique’s widely used name.

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