27565-41-9

Basic information

• Product Name: DL-Dithiothreitol
• Synonyms: DTT-MBG;DTT (RACEMIC);DL-THREO-2,3-DIHYDROXY-1,4-DITHIOLBUTANE;DL-THREO-1,4-DIMERCAPTO-2,3-BUTANEDIOL;DL-DITHIOTHREITOL;DL-DTT;DITHIOTHREITOL, 1,4-;DITT
• CAS NO: 27565-41-9
• Molecular Formula: C₄H₁₀O₂S₂
• Molecular Weight: 154.25
• EINECS: 222-468-7
• Product Categories: Biochemistry;O-Substituted Sugars;Sugar Alcohols;Sugars;Reagents for Electrophoresis
• Mol File: 27565-41-9.mol

Chemical Properties

• Melting Point: 41-44 °C(lit.)
• Boiling Point: 125-130 °C (2 mmHg)
• Flash Point: >230 °F
• Appearance: White/Liquid
• Density: 1.04 g/mL at 20 °C
• Refractive Index: 1.5200 (estimate)
• Storage Temp.: 2-8°C
• Solubility: H2O: 50 mg/mL, clear, colorless
• Water Solubility: Soluble
• Merck: 3376
• CAS DataBase Reference: DL-Dithiothreitol(CAS DataBase Reference)
• NIST Chemistry Reference: DL-Dithiothreitol(27565-41-9)
• EPA Substance Registry System: DL-Dithiothreitol(27565-41-9)

Safety Data

• Hazard Codes: Xn
• Statements: 25-36/37/38-22
• Safety Statements: 26-45-36
• WGK Germany: 3
• RTECS: EK1610000
• F: 3-10-16-23
• Hazardous Substances Data: 27565-41-9(Hazardous Substances Data)

Usage

Uses

Used in Biochemical Research:
DL-Dithiothreitol is used as a reagent for the quantitative reduction of disulfide groups in proteins. This is essential for studying the structure and function of proteins, as well as for preventing unwanted disulfide bond formation during protein manipulation.
Used in Extraction of Cholecystokinin:
DL-Dithiothreitol is used as an antioxidant to prevent the oxidation of cholecystokinin during its extraction from brain and duodenal tissues. This ensures the integrity and stability of the extracted cholecystokinin, which is crucial for accurate research and analysis.
Used in Cleavage of Disulfide Bonds:
DL-Dithiothreitol is used as a reducing agent for the cleavage of disulfide bonds in proteins. This is important for protein folding studies, as well as for the production of recombinant proteins in biotechnology applications.
Used as a Protective Agent for Thiol Groups:
DL-Dithiothreitol is a cell-permeable protective agent for thiol groups, which are essential for the proper functioning of many proteins. By protecting these thiol groups, DTT helps maintain the activity and stability of proteins in various cellular processes.

Preparation

The preparation of DL-Dithiothreitol is as follows:To a round bottom flask was charged THPP (23mg, 0.11mmol, 1.10eq) and the basic buffer solution [tris-(hydroxymethyl)-aminomethane-CaCl2 based buffer; pH 8.00; 1.0mL]. The reaction mixture was stirred at room temperature for about 5 min and then to this homogenous solution was charged trans-4,5-Dihydroxy-1,2-dithiane (15.2mg, 0.10 mmol, 1.00eq.). The reaction mixture was stirred at room temperature until the reaction was complete (about 30 min). The product was readily identified by 1H-NMR analysis.

Purification Methods

Crystallise DTT from ether and sublime it at 37o/0.005mm. It should be stored at 0o. [Beilstein 1 III 2360.]

InChI:InChI=1/C4H10O2S2/c1-2(5)3(6)4(7)8/h2-8H,1H3

Upstream product

• 462-20-4 dihydrolipoic acid 
• 16096-98-3 trans-1,2-dithiane-4,5-diol 
• 131760-67-3 N,N'-dimethyl-N,N'-bis(mercaptoacetyl)hydrazine 
• 93464-95-0 d(-Cys-Gly) 
• 38705-47-4 2-Mercaptoethyl Thioglycolate 
• 145626-87-5 Bis(2-mercaptoethyl) Sulfone 
• 145626-90-0 N,N'-Bis(2-mercaptoacetyl)-N-tert-butylhydrazine 
• 145626-92-2 1,2-Bis(mercaptomethyl)-4-methylurazole 
• 145626-89-7 N,N'-Bis(2-mercaptoacetyl)hexahydropyridazine 
• 145626-91-1 N,N'-Dicarbethoxy-N,N'-bis(mercaptomethyl)hydrazine 
• 145626-88-6 N,N'-Dicarbomethoxy-N,N'-bis(mercaptomethyl)ethylenediamine 
• 60-24-2 2-hydroxyethanethiol 
• 930-22-3 epoxybutene 
• 564-00-1 1,2:3,4-Diepoxybutane 

Downstream Products

• 74185-01-6 4,5-dihydroxy-1,2-dithiane 
• 108-98-5 thiophenol 
• 116504-33-7 <2>(2,6)Naphthalino<2>paracyclophan-1,11-dien 
• 882-33-7 diphenyldisulfane 
• 462-20-4 dihydrolipoic acid 
• 16096-98-3 trans-1,2-dithiane-4,5-diol 
• 27550-66-9 4-hydroxy-1,2-dithiolane 
• 70-18-8 glutathion 
• 60-24-2 2-hydroxyethanethiol 
• 131760-67-3 N,N'-dimethyl-N,N'-bis(mercaptoacetyl)hydrazine 
• 93464-95-0 d(-Cys-Gly) 
• 38705-47-4 2-Mercaptoethyl Thioglycolate 
• 145626-87-5 Bis(2-mercaptoethyl) Sulfone 
• 145626-90-0 N,N'-Bis(2-mercaptoacetyl)-N-tert-butylhydrazine 

Relevant articles and documents

Syntheses and Structural Characterization of Water-Soluble Selenium Reagents for the Redox Control of Protein Disulfide Bonds

A new class of water-soluble redox reagents (1-4) that contain selenium as the active site was developed for the purpose of the redox control of protein structures. The X-ray crystallographic analyses revealed that trans-3,4-dihydroxy-1-selenolane (DHSred) (1) and its Se-oxide (DHSox) (2) have two axial hydroxy groups on the selenolane five-membered ring, whereas trans-1,2-diselenane-4,5-diol (DSTox) (3), a selenium analog of oxidized dithiotreiotol (DDTox), has two equatorial hydroxy groups on the diselenane six-membered ring. According to the vicinal 3JHH coupling constants observed for 1-3, it was suggested that they adopt similar structures in solution to those in the solid state. Diselenothreitol (DSTred (4), a selenium analog of dithiothreitol (DTTred), was also synthesized, but it was too air sensitive to be isolated. The reactions of 1-4 with DTTox and DTTred indicated that the oxidizing power of DHSox (2) exceeds by far that of DTTox, while the reducing power of DSTred (4) exceeds that of DTTred.

Selective, Modular Probes for Thioredoxins Enabled by Rational Tuning of a Unique Disulfide Structure Motif

Specialized cellular networks of oxidoreductases coordinate the dithiol/disulfide-exchange reactions that control metabolism, protein regulation, and redox homeostasis. For probes to be selective for redox enzymes and effector proteins (nM to μM concentrations), they must also be able to resist non-specific triggering by the ca. 50 mM background of non-catalytic cellular monothiols. However, no such selective reduction-sensing systems have yet been established. Here, we used rational structural design to independently vary thermodynamic and kinetic aspects of disulfide stability, creating a series of unusual disulfide reduction trigger units designed for stability to monothiols. We integrated the motifs into modular series of fluorogenic probes that release and activate an arbitrary chemical cargo upon reduction, and compared their performance to that of the literature-known disulfides. The probes were comprehensively screened for biological stability and selectivity against a range of redox effector proteins and enzymes. This design process delivered the first disulfide probes with excellent stability to monothiols yet high selectivity for the key redox-Active protein effector, thioredoxin. We anticipate that further applications of these novel disulfide triggers will deliver unique probes targeting cellular thioredoxins. We also anticipate that further tuning following this design paradigm will enable redox probes for other important dithiol-manifold redox proteins, that will be useful in revealing the hitherto hidden dynamics of endogenous cellular redox systems.

Charge Accumulation and Multi-Electron Photoredox Chemistry with a Sensitizer–Catalyst–Sensitizer Triad

Photoinduced electron transfer in donor–sensitizer–acceptor compounds usually leads to simple electron–hole pairs, and photoredox catalysis typically relies on single-electron transfer (SET) events. This work reports on a molecular triad able to accumulate two electrons on a central dibenzo[1,2]dithiin moiety flanked by two peripheral RuII photosensitizers. Under continuous illumination, the doubly reduced form of the dibenzo[1,2]dithiin undergoes thiolate–disulfide exchange with an aliphatic disulfide substrate, thereby acting as a two-electron catalyst after two initial SET events with triethylamine at the RuII sensitizers. The use of a relatively simple triad for coupling two separate SET processes to a subsequent two-electron reduction is an important conceptual advance from photoinduced SET and light-driven charge accumulation towards multi-electron photoredox catalysis. This is relevant for artificial photosynthesis and light-driven multi-electron chemistry in general.

Tris(3-hydroxypropyl)phosphine (THPP): A mild, air-stable reagent for the rapid, reductive cleavage of small-molecule disulfides

Tris(3-hydroxypropyl)phosphine (THPP) is demonstrated to be a versatile, water-soluble and air-stable reducing agent, allowing for the rapid, irreversible reductive cleavage of disulfide bonds in both aqueous and buffered aqueous-organic media. The reagent shows exceptional stability at biological pH under which condition it permits the rapid reduction of a wide range of differentially functionalized small-molecule disulfides.

Thiols and selenols as electron-relay catalysts for disulfide-bond reduction

Pass them on! Dithiobutylamine immobilized on a resin is a useful reagent for the reduction of disulfide bonds. Its ability to reduce a disulfide bond in a protein is enhanced greatly if used along with a soluble strained cyclic disulfide or mixed diselenide that relays electrons from the resin to the protein. This electron-relay catalysis system provides distinct advantages over the use of excess soluble reducing agent alone. Copyright

METHOD FOR THE PRODUCTION OF BISEPOXIDES AND DITHIOLS

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Micellar systems

A complex is described that is deliverable to a cell comprising inserting a nucleic acid or other cargo into a reverse micelle. The reverse micelle has the property to compact the nucleic acid for easier delivery.

4-hydroxyquinoline-3-carboxamides and hydrazides as antiviral agents

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Interleukin-2/viral antigen protein chimers

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BIOLOGICALLY ACTIVE COMPOUNDS ISOLATED FROM AEROBIC FERMENTATION OF TRICHODERMA VIRIDE

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