The full form of DTT is Dithiothreitol.
Dithiothreitol (DTT), also known as Cleland's reagent, is a small molecule redox reagent often used in biochemical applications to reduce disulfide bonds and maintain proteins in their reduced form. Its oxidized form is a disulfide-bonded 6-membered ring. DTT is widely utilized in laboratories due to its effectiveness and stability.
Here's a breakdown of its key aspects:
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Function: DTT is primarily used as a reducing agent. It can break disulfide bonds in proteins and peptides, preventing them from forming unwanted aggregates and ensuring they remain in their active conformation.
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Mechanism: DTT works by donating electrons to disulfide bonds, converting them into free thiol groups.
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Applications: Common applications of DTT include:
- Protein Biochemistry: Maintaining proteins in a reduced state during purification, storage, and analysis.
- Molecular Biology: Denaturing proteins for SDS-PAGE.
- Cell Biology: Reducing disulfide bonds in cell lysates for protein extraction.
- Pharmaceuticals: Stabilizing therapeutic proteins.
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Alternatives: While DTT is commonly used, other reducing agents like 2-Mercaptoethanol (BME) and Tris(2-carboxyethyl)phosphine (TCEP) can also be used depending on the application. TCEP is often preferred because it's odorless and a stronger reducing agent at lower pH.
