dithiothreitol

🔬 Dithiothreitol (DTT) — Overview

Chemical Identity

Name: 1,4-Dithiothreitol (DTT)
Synonyms: Cleland’s Reagent
Molecular Formula: C₄H₁₀O₂S₂
CAS Number: 3483-12-3
Molecular Weight: 154.25 g/mol
Appearance: White crystalline powder
Purity: ≥ 99%
UV Absorbance: < 0.1 at 280 nm for a 1% solution
Storage: Store at –20 °C
Solubility: Highly soluble in water, ethanol, chloroform, ether, and ethyl acetate

Dithiothreitol (DTT) is a potent reducing agent widely utilized in various biochemical and molecular biology applications

Reduction of Disulfide Bonds: DTT effectively reduces disulfide bonds in proteins and peptides, maintaining them in their reduced state. This property is crucial for protein denaturation and analysis.
Protein Stabilization: By preserving thiol groups in their reduced form, DTT stabilizes enzymes and other proteins, preventing unwanted oxidation.
Electrophoresis: DTT is commonly used in SDS-PAGE sample buffers to break disulfide linkages, ensuring proteins are fully denatured for accurate molecular weight determination.
Cleavage of Cross-Linkers: It can reduce disulfide bridges in cross-linkers like N,N′-bis(acryloyl)cystamine, aiding in the disruption of polyacrylamide gel matrices.

Redox Potential: DTT has a redox potential of –0.33 V at pH 7, indicating its strong reducing capability.
Molecular Structure: Consists of two thiol (–SH) groups attached to a four-carbon backbone, classifying it as a dithiol and a diol.

Astor Scientific offers DTT in various quantities:

For more details and to purchase, visit:
👉 DTT, 1,4-Dithiothreitol – Astor Scientific

Feature	Details
Product	DTT, 1,4-Dithiothreitol
Purity	≥ 99%
UV Absorbance	< 0.1 at 280 nm for 1% solution
Redox Potential	–0.33 V at pH 7
Storage	–20 °C
Applications	Reduction of disulfide bonds, protein stabilization, electrophoresis, etc.