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Dithiothreitol (DTT)
Disufide crosslinks of cystines in proteins can be reduced to cysteine residues by dithiothreitol (DTT).Read more
| Catalog Number | Quantity |
|---|---|
| D1532 | 1 g |
Catalog number D1532
Price (USD)
124.00
Each
In stock
Quantity:
1 g
Price (USD)
124.00
Each
Disufide crosslinks of cystines in proteins can be reduced to cysteine residues by dithiothreitol (DTT).
For Research Use Only. Not for use in diagnostic procedures.
Specifications
FormSolid
Quantity1 g
Shipping ConditionRoom Temperature
Product TypeDithiothreitol
Unit SizeEach
Contents & Storage
Store at room temperature.
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Lot #Certificate TypeDateCatalog Number(s)
3141715Certificate of AnalysisMar 31, 2025D1532
3154561Certificate of AnalysisMar 31, 2025D1532
3135776Certificate of AnalysisMar 27, 2025D1532
3012681Certificate of AnalysisOct 21, 2024D1532
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Safety Data Sheets
SDSMolecular Probes® Handbook
Frequently asked questions (FAQs)
Either BME or DTT can be used in the NuPAGE LDS Sample Buffer.
Make sure that a fresh solution of BME is used. FINAL concentration:
DTT 50-100 mM
BME 2-5%
Find additional tips, troubleshooting help, and resources within our Protein Electrophoresis and Western Blotting Support Center.
Preparing 1 M DTT:
1) Dissolve 3.09 g DTT in 20 mL distilled H2O.
2) Dispense into 1 mL aliquots.
3) Store the aliquots at -20 degrees C.
Note: Upon thawing the vial, there may be some precipitation that can be re-dissolved by warming and mixing.
Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.
Citations & References (17)
Search citations by name, author, journal title or abstract text
Citations & References
Abstract
Introduction of sulfhydryl groups into proteins at carboxyl sites.
Journal:Biochim Biophys Acta
PubMed ID:2160279
'A two-step procedure for introduction of sulfhydryl groups at protein carboxyl groups is described. The resultant proteins contain 2-aminoethanethiol residues bound by amide linkages to the protein carboxyl groups. First an amide bond is formed between a carboxyl group of the protein and one of the amino groups of cystamine.
Simple alkanethiol groups for temporary blocking of sulfhydryl groups of enzymes.
Journal:Biochemistry
PubMed ID:163643
'New reagents for the temporary blocking of active or accessible sulfhydryl groups of enzymes have been developed. These reagents, which are either alkyl alkanethiolsulfonates or alkoxycarbonylalkyl disulfides, rapidly and quantitatively place various RS- groups on the sulfhydryls to generate mixed disulfides. In all cases native enzymes can be regenerated with
An introduction to methods for analyzing thiols and disulfides: Reactions, reagents, and practical considerations.
Journal:Anal Biochem
PubMed ID:19664585
'This review outlines the basic issues to consider when dealing with biochemical and cellular aspects of thiol–disulfide chemistry. The overall focus is on practical aspects, including typical biochemical experimental conditions and caveats to consider in interpreting results. Reagents for thiol derivatization and disulfide reduction are evaluated and compared, and we
Measurement of cyst(e)amine in physiological samples by high performance liquid chromatography.
Journal:Anal Biochem
PubMed ID:3394941
'Two methods for measurement of cyst(e)amine in physiological samples are described. One method involves reduction of disulfides present in the sample with tributylphosphine, reversed phase chromatography of thiols, and electrochemical detection of cysteamine and other thiols. The other method involves reduction of disulfides with dithiothreitol, derivatization of thiols with 7-diethylamino-3-(4''-maleimidylphenyl)-4-methylcoumarin,
Chemical reduction of disulfides.
Journal:Methods Enzymol
PubMed ID:3657541
17 total citations