DL-Dithiothreitol 

Tested for use in reduced SDS-PAGE

An excellent reagent for maintaining SH groups in reduced state;?? quantitatively reduces disulfides. DTT is effective in sample buffers for reducing protein disulfide bonds prior to SDS-PAGE. DTT can also be used for reducing the disulfide bridge of the cross-linker N,N′-bis(acryloyl)cystamine to break apart the matrix of a polyacrylamide gel. DTT is less pungent and is less toxic than 2-mercaptoethanol. Typically, a seven fold lower concentration of DTT (100 mM) is needed than is used for 2-mercaptoethanol (5% v/v, 700 mM).

for electrophoresis

≥99%

40-44 °C

41-44 °C(lit.)

heavy metals (as Pb): <10 ppm

A0.02M/280 <0.04

2-8°C

Cleland, W.W. Biochemistry 3, 480, (1964) abstract

Sears, D.W., In the investigation of incremental and kinetic reduction in proteins. Biochemistry 16, 2031, (1977)

Ruegg, U.T., Cleavage of disulfide bonds in proteins. Meth. Enzymol. 47, 111, (1977)

MacDonald, R.J., Isolation of RNA using guanidinium salts. Inclusion of a reductant enhances denaturation by breaking intramolecular protein disulfide bonds. Meth. Enzymol. 152, 219, (1987)

Jabusch, J.R., In protein sequence analysis. Anal. Biochem. 91, 532, (1978)

Bacarese-Hamilton, A., Prevents the oxidation of cholecystokinin during its extraction from brain and duodenal tissues. Ann. N.Y. Acad. Sci. 448, 571, (1985)

Merck 13,3412

Beil. 1,III,2360

Aldrich MSDS 1, 840:C / Corp MSDS 1 (1), 1483:A / FT-IR 2 (1), 417:D / FT-IR 1 (1), 263:C / FT-NMR 1 (1), 424:A / IR-Spectra (3), 155:E / IR-Spectra (2), 139:A / NMR-Reference 2 (1), 230:B / RegBook 1 (1), 283:C / Sigma FT-IR 1 (2), 534:A / Structure Index 1, 38:E:8

3

EK1610000

235.4

113