2-Mercaptoethanol

2-Mercaptoethanol is a small sulfur-containing organic compound with a thiol group and a hydroxyl group. It reduces disulfide bonds, making it useful in protein chemistry and laboratory reagents.

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Disulfide bond: A covalent bond between the sulfur atoms of two cysteine residues or other thiols. 2-Mercaptoethanol reduces these bonds to free thiols in proteins.
Sodium dodecyl sulfate–polyacrylamide gel electrophoresis: A method that separates proteins mainly by molecular mass using an SDS-containing polyacrylamide gel. 2-Mercaptoethanol reduces disulfides before electrophoresis, helping separate protein subunits.
Ethanol: A two-carbon alcohol with the formula C₂H₅OH. 2-Mercaptoethanol has a related two-carbon skeleton, with sulfur replacing one oxygen.
Tris(2-carboxyethyl)phosphine: A water-soluble phosphine reducing agent used to cleave disulfide bonds. Unlike 2-mercaptoethanol, it is odorless and does not contain a thiol group.
Thiol: An organic functional group containing a sulfur–hydrogen bond, written –SH. Its thiol group supplies the reducing chemistry of 2-mercaptoethanol.
Laemmli buffer: A protein sample buffer containing SDS, buffer, tracking dye, and commonly a reducing agent. It is a common preparation in which 2-mercaptoethanol helps denature proteins.
Functional group: A set of atoms in a molecule that largely determines its characteristic chemical reactions. Its hydroxyl and thiol groups give 2-mercaptoethanol distinct properties.
Cysteamine: A small molecule containing both an amine and a thiol group. It is another biologically relevant thiol, but its amine changes its chemical behavior.
Redox reaction: A chemical reaction involving transfer of electrons between substances. Reduction of disulfides by 2-mercaptoethanol is an electron-transfer process.
Protein denaturation: The loss of a protein's native structure without necessarily breaking its peptide bonds. Disulfide reduction by 2-mercaptoethanol can disrupt structural constraints during denaturation.