Dithiothreitol (DTT)

SKU
C-1029
  • CAS:3483-12-3
  • Formula:C4H10O2S2
  • MW:154.25 Da
  • Appearance:White crystalline powder
  • Purity:≥99.0%

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Starting at $32.99

Product Name Qty
Dithiothreitol, DTT
5 g
$32.99
Dithiothreitol, DTT
10 g
$44.99
Dithiothreitol, DTT
100 g
$334.99
Dithiothreitol, DTT
1 kg
$1,499.99

Description

Dithiothreitol (DTT), is a small-molecule redox reagent, known as Cleland's reagent, that forms a six-member ring with an internal disulfide bond. It has a redox potential of -0.33 V at pH 7. The reduction of typical disulfide bond proceeds by two sequential thiol-disulfide exchange reactions. DTT is effective in buffers to reduce protein disulfide bonds prior to SDS-PAGE. It can protect protein sulfhydryls and restore enzyme activity lost by oxidation.

Applications

• For reducing or "deprotecting" agent for thiolated DNA
• For reducing disulfide bonds of proteins
• Used as an oxidizing agent
• Used as a component of medium for the demembranation and reactivation of spermatozoa
• Used to prevent intramolecular and intermolecular disulfide bonds from forming between cysteine residues of proteins

 

More Information
Alternate Name/Synonyms
DTT; Cleland's Reagent
SKU
C-1029
CAS #
3483-12-3
Chemical Name
(2S,3S)-1,4-bis(sulfanyl)butane-2,3-diol
Chemical Formula
C4H10O2S2
Molecular Weight
154.25 Da
Appearance
White crystalline powder
Purity
≥99.0%
Solubility
10% solution in water. Clear and colorless
Melting Point
42-43°C
Preparation
N/A
Storage Temp
+4°C, under inert gas, desiccated
THERAPEUTIC AREA
Not Applicable
USE
DTT is frequently used to reduce the disulfide bonds of proteins and, more generally, to prevent intramolecular and intermolecular disulfide bonds from forming between cysteine residues of proteins. However, even DTT cannot reduce buried (solvent-inaccessible) disulfide bonds, so reduction of disulfide bonds is sometimes carried out under denaturing conditions (e.g., at high temperatures, or in the presence of a strong denaturant such as 6 M guanidinium chloride, 8 M urea, or 1% sodium dodecylsulfate). DTT is oftentimes used along with sodium dodecylsulfate in SDS-PAGE to further denature proteins by reducing their disulfide bonds to allow for better separation of proteins during electrophoresis. Because of the ability to reduce disulfide bonds, DTT can be used to denature CD38 on red blood cells. Conversely, the solvent exposure of different disulfide bonds can be assayed by their rate of reduction in the presence of DTT. DTT can also be used as an oxidizing agent. Its principal advantage is that effectively no mixed-disulfide species are populated, in contrast to other agents such as glutathione. In very rare cases, a DTT adduct may be formed, i.e., the two sulfur atoms of DTT may form disulfide bonds to different sulfur atoms; in such cases, DTT cannot cyclize since it has no such remaining free thiols.
Merck Index
12.3441.1996
MDL NUMBER
MFCD00004877
CHEMACX
X1009950-2
INCHI
InChI=1S/C4H10O2S2/c5-3(1-7)4(6)2-8/h3-8H,1-2H2/t3-,4-/m1/s1
SMILES
C([C@H]([C@@H](CS)O)O)S
RTECS
EK1610000
UN #'S
UN 3335
PACKING GROUP
III
Handling
Hygroscopic. Protect from moisture. Protect from light. The pharmacological and toxicological properties of this product have not been fully investigated. Use caution when handling. Do not use this compound if you are not fully trained or are unaware of the hazards involved.
Certificate of Analysis 1
Certificate of Analysis 2
Certificate of Analysis 3
GHS PICTOGRAMS
Handling Hygroscopic. Protect from moisture. Protect from light. The pharmacological and toxicological properties of this product have not been fully investigated. Use caution when handling. Do not use this compound if you are not fully trained or are unaware of the hazards involved.
UN #'S UN 3335
Packing Group III
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