DL-1,4-Dithiothreitol: Your Essential Reducing Agent for Research

Discover the power of DL-1,4-Dithiothreitol in maintaining protein integrity and enhancing biochemical processes.

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Key Advantages

Superior Reduction Power

As a potent reducing agent, DL-1,4-Dithiothreitol effectively cleaves disulfide bonds, essential for processes like protein renaturation and preventing aggregation in biomolecular research.

Enhanced Protein Stability

By maintaining SH groups in their reduced state, DTT plays a vital role in maintaining protein stability and preventing the loss of biological activity, a critical factor in experimental design.

Broad Applicability

The versatility of DTT extends across numerous applications, from enzyme assays and electrophoresis to protecting thiol-containing compounds from oxidation, making it a staple in molecular biology labs.

Key Applications

Biochemistry & Molecular Biology

DL-1,4-Dithiothreitol is indispensable for maintaining the reduced state of thiol groups, crucial for experiments studying protein structure, function, and interactions.

Protein Folding Studies

It aids in preventing incorrect disulfide bond formation, thereby facilitating correct protein folding and ensuring the biological activity of recombinant proteins.

Enzyme Stability Enhancement

DTT protects enzymatic activity by keeping essential cysteine thiol groups in their reduced state, which is critical for enzyme kinetics and stability assays.

RNA and DNA Research

Used to prevent nucleic acid oxidation and degradation, ensuring the integrity of genetic material during isolation, manipulation, and analysis.