1,4-Dithio-DL-threitol is a sulfur-containing, DL-configured dithiol compound featuring a four-carbon backbone with two thiol groups masked as a dithio (thioether/thiol-equivalent) functionality, placing it in the class of redox-active amino-alcohol derivatives rather than a proteinogenic amino acid. The molecule bears hydroxyl substituents and sulfur atoms that can participate in thiol-disulfide exchange chemistry after conversion to reactive thiol forms, while the DL stereochemical descriptor indicates racemic composition at the relevant stereocenters. In biochemical and synthetic workflows, it is used as a reducing or thiol-transfer reagent to generate sulfhydryl functionality for disulfide bond formation or cleavage control, and it can serve as a chemical handle in labeling, peptide or protein modification, and preparation of thiol-containing intermediates.
CAT No: CP27037
CAS No:3483/12/3
Synonyms/Alias:Clelands Reagent;Dithiothreitol,DTT
1,4-Dithio-DL-threitol is a DL-threitol-derived dithiol reagent in which two thiol groups are present as a reducing functionality for thiol-disulfide exchange chemistry. It is commonly used in protein chemistry and peptide workflows where controlled reduction of disulfide bonds or maintenance of cysteine residues in a reduced state is required. As a small, sulfur-rich organic reductant, it supports downstream handling of thiol-containing biomolecules and can be paired with disulfide formation or thiol quantification steps in analytical and synthesis pipelines.
1. Disulfide Reduction Workflows
1,4-Dithio-DL-threitol is used to reduce disulfide bonds in peptides and proteins during sample preparation for biochemical assays and structural studies. Researchers in protein chemistry and chemical biology rely on it to generate free thiols from oxidized cystine/disulfide forms, enabling subsequent alkylation, conjugation, or controlled re-oxidation steps. Its dithiol character supports efficient thiol-disulfide exchange, making it a practical reagent when maintaining cysteine reactivity is important for downstream derivatization or binding studies.
2. Thiol-Functionalization Preparation
1,4-Dithio-DL-threitol is frequently incorporated into workflows that prepare thiol-reactive biomolecules for site-directed labeling and chemical modification. In peptide synthesis and post-synthetic modification programs, it helps ensure that cysteine-containing intermediates or purified peptides carry accessible thiol groups prior to reaction with electrophilic labeling reagents. This is particularly valuable when the target conjugates require consistent thiol availability to improve reproducibility across batches in research-grade bioconjugation and analytical method development.
3. Protein Sample Handling Standards
1,4-Dithio-DL-threitol is used as a reducing component in protein sample processing where the goal is to standardize the redox state before electrophoresis, immunoblotting, or mass spectrometry-compatible preparation. Proteomics and protein analytics teams often include dithiol reductants to reduce disulfide-linked heterogeneity and to improve comparability of thiol-containing species across timepoints and experimental conditions. The reagent's small-molecule nature also makes it straightforward to include in buffer systems used for analytical sample standardization and thiol state control.
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