Dithiothreitol (DTT)
Dithiothreitol (DTT)
Invitrogen™

Dithiothreitol (DTT)

Disufide crosslinks of cystines in proteins can be reduced to cysteine residues by dithiothreitol (DTT).Read more
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Catalog NumberQuantity
D15321 g
Catalog number D1532
Price (KRW)
132,000
キャンペーン価格
Ends: 31-Dec-2025
165,000
Save 33,000 (20%)
Each
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Quantity:
1 g
Price (KRW)
132,000
キャンペーン価格
Ends: 31-Dec-2025
165,000
Save 33,000 (20%)
Each
Add to cart
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.

Frequently asked questions (FAQs)

Can beta-mercaptoethanol (BME) be used rather than DTT as the reducing agent in the NuPAGE LDS Sample Buffer?

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.

How do I prepare a 1 M DTT solution from powder and how should I store the solution?

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)

Citations & References
Abstract
Introduction of sulfhydryl groups into proteins at carboxyl sites.
Authors:Lin CM, Mihal KA, Krueger RJ
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. ... More
Simple alkanethiol groups for temporary blocking of sulfhydryl groups of enzymes.
Authors:Smith DJ, Maggio, ET, Kenyon GL
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 ... More
An introduction to methods for analyzing thiols and disulfides: Reactions, reagents, and practical considerations.
Authors:Hansen RE, Winther JR,
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 ... More
Measurement of cyst(e)amine in physiological samples by high performance liquid chromatography.
Authors:Garcia RA, Hirschberger LL, Stipanuk MH
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, ... More
Chemical reduction of disulfides.
Authors:Jocelyn PC
Journal:Methods Enzymol
PubMed ID:3657541