Description
GoldBio's DTT (Dithiothreitol), a ≥99% pure and protease-free reducing agent, is essential for maintaining thiol integrity and preventing oxidative damage in molecular biology, biochemistry, and proteomics workflows. Ideal for disulfide bond reduction during SDS-PAGE, RNA isolation, or protein purification, DTT ensures the stability and functionality of enzymes, redox-sensitive proteins, and nucleic acids. Trusted by researchers for its high purity and consistency, GoldBio’s DTT provides the reliability required in redox biology, enzyme assays, and thiol-sensitive systems. Make it your go-to reagent for uncompromised redox control in the lab.
DTT is a nearly 7-fold stronger reduction agent than βME (β-mercaptoethanol) and has a less offensive odor and is less toxic.
N.B.
During the summer (between 5/1 and 9/30), GoldBio may require shipment by Next Day Air with blue ice in order to avoid high temperatures that may adversely affect DTT quality.
Applications
- PROTEASE FREE Oxidizing agent
- Reducing agent for polyacrylamide gels
- Denaturation of protein and peptide disulfide bond
- Sperm cell lysis
- Stabilizer for specific enzymes; i.e. Taq polymerase and restriction digest enzymes
- Protects from oxidation damage in lysis buffers
Common Research Applications
(Click each for more information)
Reducing Agent in Protein Denaturation and Sample Preparation
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Purpose: To reduce disulfide bonds in proteins, ensuring complete denaturation prior to electrophoresis or mass spectrometry.
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How It Works: DTT reduces disulfide bonds between cysteine residues, converting them to free thiol groups (-SH) and promoting linearized protein structures.
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Applications: SDS-PAGE, Western blotting, and LC-MS/MS sample preparation.
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680–685.
Stabilizing Enzymes with Free Thiols
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Purpose: To protect thiol-sensitive enzymes from oxidation that could impair activity.
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How It Works: DTT preserves sulfhydryl (-SH) groups in their reduced, active form during purification and assay conditions.
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Applications: Enzyme assays, protease stabilization, and recombinant enzyme purification.
Moss, M. L., & Lambert, M. H. (2002). Shedding of membrane proteins by ADAM family proteases. Essays in Biochemistry, 38, 141–153.
Protecting Thiol Groups During Protein Purification and Storage
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Purpose: To maintain protein solubility and prevent disulfide-mediated aggregation during purification workflows.
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How It Works: DTT acts as a reducing agent in lysis and purification buffers, keeping cysteine residues in a reduced state.
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Applications: His-tag/Ni-NTA purification, MBP or SUMO fusion systems, and protein storage buffers.
Kapust, R. B., & Waugh, D. S. (1999). Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Science, 8(8), 1668–1674.
Preventing Oxidative Damage in RNA Isolation and Storage
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Purpose: To prevent RNA degradation by RNases and oxidative damage during extraction and storage.
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How It Works: DTT inactivates RNases by reducing essential disulfide bonds and acts as an antioxidant in extraction buffers.
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Applications: RNA isolation, RT-PCR, Northern blotting, and transcriptomic workflows.
Chomczynski, P., & Sacchi, N. (1987). Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Analytical Biochemistry, 162(1), 156–159.
Assays Requiring a Reducing Environment (e.g., Thioredoxin, Redox Sensors)
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Purpose: To simulate intracellular reducing conditions for studying redox-active enzymes and probes.
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How It Works: DTT donates reducing equivalents to maintain proteins and redox sensors in their reduced, active forms.
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Applications: Redox enzyme assays, oxidative stress studies, and fluorescent redox probe systems.
Holmgren, A. (1979). Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. Journal of Biological Chemistry, 254(19), 9627–9632.
Benefits
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Preferred alternative to β-mercaptoethanol: Lower odor, higher stability in certain systems, and less volatility.
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High reliability in redox-sensitive workflows: Ensures complete reduction of disulfide bonds in protein and nucleic acid preparations.
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Wide applicability: Used across protein purification, enzymology, RNA work, and redox biology.
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Protease-free formulation: Suitable for sensitive protein-based applications without proteolytic degradation risk.
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Predictable behavior and solubility: Easily soluble and well characterized, making experimental planning straightforward.
Storage/Handling
Store desiccated at -20°C. Solutions should be prepared fresh, daily.
Working Concentration
DTT is commonly stored in a 1M stock solution for up to 1 year at -20°C.
Working concentrations are typically 1-10mM and should be remade daily.
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