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D9779

Sigma-Aldrich

DL-Dithiothreitol

for molecular biology, ≥98% (HPLC), ≥99% (titration)

Synonym(s):

(±)-Dithiothreitol, rac-Dithiothreitol, Dithiothreitol, threo-1,4-Dimercapto-2,3-butanediol, Cleland’s reagent, DTT

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About This Item

Linear Formula:
HSCH2CH(OH)CH(OH)CH2SH
CAS Number:
Molecular Weight:
154.25
Beilstein:
1719757
EC Number:
MDL number:
UNSPSC Code:
12161504
PubChem Substance ID:
NACRES:
NA.31

grade

for molecular biology

Assay

≥98% (HPLC)
≥99% (titration)

form

powder

reaction suitability

reagent type: reductant

mp

41-44 °C (lit.)

solubility

H2O: 50 mg/mL

cation traces

heavy metals (as Pb): ≤5 ppm

suitability

suitable for molecular biology

foreign activity

DNase, RNase, protease, none detected

storage temp.

2-8°C

SMILES string

O[C@H](CS)[C@H](O)CS

InChI

1S/C4H10O2S2/c5-3(1-7)4(6)2-8/h3-8H,1-2H2/t3-,4-/m1/s1

InChI key

VHJLVAABSRFDPM-QWWZWVQMSA-N

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General description

Dithiothreitol (DTT) is an excellent reagent for maintaining SH groups in a reduced state in proteins. It initiates the thiol-disulfide exchange reaction to completely reduce the intra-or inter-molecular disulfide bonds in biomolecules. DTT specifically targets the disulfide bridge of the cross-linker N,N′-bis(acryloyl)cystamine to break apart the matrix of a polyacrylamide gel and sodium dodecyl polyacrylamide gel electrophoresis (SDS-PAGE). Hence, it is highly effective in use with buffers that quantitatively reduce disulfides. DTT is less pungent and less toxic in nature than 2-mercaptoethanol. It is also 7x more concentrated than beta-mercaptoethanol.

Application

DL-Dithiothreitol is used in protein samples to reduce the disulfide bonds before loading the sample onto the gel for Western Blot or SDS-PAGE It has been used in the procedure of in situ hybridization of mRNA.

It has been used:
  • as a component for protein extraction in western blot analysis
  • to prepare sample lysis buffer for quantitative mass spectroscopy
  • as a kinase buffer component for enzyme-linked immunosorbent assay (ELISA)
An excellent reagent for maintaining SH groups in reduced state; quantitatively reduces disulfides. DTT is effective in sample buffers for reducing protein disulfide bonds prior to SDS-PAGE. DTT can also be used for reducing the disulfide bridge of the cross-linker N,N′-bis(acryloyl)cystamine to break apart the matrix of a polyacrylamide gel. DTT is less pungent and is less toxic than 2-mercaptoethanol. Typically, a seven fold lower concentration of DTT (100 mM) is needed than is used for 2-mercaptoethanol (5% v/v, 700 mM).

Biochem/physiol Actions

Dithiothreitol (DTT) is frequently utilized in biochemical preparations of thiol proteins and chemical peptide synthesis. DTT is also used in protein chemistry research on the folding of proteins and enzyme activity.

Features and Benefits

  • Suitable for molecular biology
  • RNase, DNase, Exonuclease, and Protease-free
  • High purity (HPLC ≥98%)
  • No heavy metal ≤5ppm

Other Notes

For additional information on our range of Biochemicals, please complete this form.

Pictograms

CorrosionExclamation mark

Signal Word

Danger

Hazard Statements

Hazard Classifications

Acute Tox. 4 Oral - Eye Dam. 1 - Skin Irrit. 2

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Protocols

Follow this DDT reduction protocol to reduce disulfide bonds in thiol-modified oligonucleotides.

Follow this DDT reduction protocol to reduce disulfide bonds in thiol-modified oligonucleotides.

Follow this DDT reduction protocol to reduce disulfide bonds in thiol-modified oligonucleotides.

Follow this DDT reduction protocol to reduce disulfide bonds in thiol-modified oligonucleotides.

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