DTT

1,4-dithiothreitol is commonly known as Cleland′s reagent. It confers protection to thiol groups and reduces disulfide bonds in peptides and proteins.[1] It reduces disulfide bonds to sulfhydryl group and is commonly used in receptor studies, to determine the functional importance of disulfide bonds during receptor occupancy and functionality.[2] It also maintains monothiols completely in the reduced state.

1,4-dithiothreitol is used in:

• Isolation, purification and characterization of proteins and enzymes[3]
• Measurement of enzyme activities (reactivation of enzymes)
• Determination of disulfide groups in proteins and enzymes
• DNA extraction prior to amplification[4]

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).

Oxidized form: <2.5% (absorbance at 283nm)

Enantiomers
Our DTT-preparation is optically inactive, i.e. it is the D,L-DTT.

Storage conditions (working solution): A solution of DTT in Hepes buffer, pH 7.75 is stable for one week at 2 to 8 °C if the container is tightly sealed and the solution is protected from atmospheric oxygen by argon or nitrogen.

For life science research only. Not for use in diagnostic procedures.