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. 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.[1] It also maintains monothiols completely in the reduced state.

1,4-dithiothreitol is used in:

• Isolation, purification and characterization of proteins and enzymes[2]
• Measurement of enzyme activities (reactivation of enzymes)
• Determination of disulfide groups in proteins and enzymes
• DNA extraction prior to amplification[3]

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)

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.

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

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