2-Mercaptoethanol 

BME is suitable for reducing protein disulfide bonds prior to polyacrylamide gel electrophoresis and is usually included in a sample buffer for SDS-PAGE at a concentration of 5%. 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.

for electrophoresis

2.69 (vs air)

1 mmHg ( 20 °C)

18 %

14.3 M (pure liquid)

n20/D 1.500(lit.)

157 °C(lit.)

1.114 g/mL at 25 °C(lit.)

Cu: <1 ppm

Fe: <1 ppm

Pb: <5 ppm

Zn: <1 ppm

Hames, B.D. and Rickwood, D. Gel Electrophoresis of Proteins: A Practical Approach 2nd ed., New York, NY , (1990), 32-35

Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685, (1970) abstract

Merck 13,5894

Beil. 1,IV,2428

Aldrich MSDS 1, 1162:C / Corp MSDS 1 (2), 2209:A / FT-IR 2 (1), 415:B / FT-IR 1 (1), 262:B / FT-NMR 1 (1), 422:B / IR-Spectra (3), 154:F / IR-Spectra (2), 138:E / NMR-Reference 2 (1), 228:B / RegBook 1 (1), 281:L / Sax 6, 1744 / Sigma FT-IR 1 (2), 700:C / Structure Index 1, 38:D:7 / Vapor Phase 3, 344:C

UN2966 6.1/PG 2

3

KL5600000

18.00%

2.30%

170.6

77