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Description
- 2-Mercaptoethanol is used to reduce disulfide linkages in solubilizing proteins for gel electrophoresis (typically used in SDS-PAGE sample buffer at 5% concentration).
- Also reduces excess oxidative polymerization of catalysts.
- Cleaving intermolecular (between subunits) disulfide bonds allows the subunits of a protein to separate independently on SDS-PAGE.
- Cleaving intramolecular (within subunit) disulfide bonds allows the subunits to become completely denatured so that each peptide migrates according to its chain length with no influence due to secondary structure.
- In solution, 2-mercaptoethanol is readily oxidized in air to a disulfide, especially at alkaline pH. Because of this property, it is widely used to protect proteins, enzymes in particular, from becoming inactive.
- An excess of 2-mercaptoethanol (generally used at 0.01 M) will maintain the protein thiol groups in their reduced state.
Solubility
- Miscible with water, alcohol, ether and benzene.
- Solutions containing even trace levels (nanomolar) of some metal salts (especially copper (II) or cobalt(II)) are unstable at pH >5 and progressively less stable at higher pH values.
- Most buffers (especially phosphate) contain enough metal salts to lead to substantial loss of -SH within 1 to 2 days.
- The addition of EDTA helps to stabilize solutions.
- If diluted product needs to be stored, it is recommended to store at pH 6 to 7 with EDTA (0.05 mM) at 2 to 8°C for no more than 2 to 3 days; however, we highly recommend adding neat 2-mercaptoethanol as needed to the sample.
Specifications
Specifications
| pH Range | 5.0 (0.1 M in water) |
| Molecular Weight (g/mol) | 78.13 g/mol |
| Purity | ≥98% |
| CAS | 60-24-2 |
| Form | Liquid |
| Boiling Point | 157°C |
| Density | 1.114 g/mL at 25°C |
| Flash Point | 68°C (154.4°F) |
| Vapor Density | 2.69 |
| Vapor Pressure | 1 mm Hg at 20°C |
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Unless specified otherwise, for research or further manufacturing use only, not for direct human use.
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