Sigma-Aldrich DL-Dithiothreitol. BioUltra, Molecular Biology, ≥99.5% (RT). 1 g

Name: Sigma-Aldrich DL-Dithiothreitol. BioUltra, Molecular Biology, ≥99.5% (RT). 1 g
SKU: SIAL-43815-1G
Price: 176.32 USD

List Price $176.32 Your Price $176.32

Sigma-Aldrich DL-Dithiothreitol. BioUltra, Molecular Biology, ≥99.5% (RT). 1 g - SIAL (Additional S&H Or Hazmat Fees May Apply)

NETA PART: SIAL-43815-1G

MFG.PART: 43815-1G

UNSPSC: 41122409

Manufacturer: Sigma-Aldrich

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Description

grade

Molecular Biology

product line

BioUltra

assay

≥99.5% (RT)

form

powder

reaction suitability

reagent type: reductant

impurities

DNases, none detected
RNases, none detected
insoluble matter, passes filter test
phosphatases, none detected
proteases, none detected
≤0.3% 4,5-dihydroxy-1,2-dithiane

pH

4.0-6.5 (25 °C, 0.1 M in H₂O)

mp

41-44 °C (lit.)

solubility

H₂O: 0.1 M at 20 °C, clear, colorless

anion traces

sulfate (SO₄^2-): ≤50 mg/kg

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Related Categories

Biochemicals

Chelating & Reducing Agents for Research

High-Purity Biochemicals and Reagents

General description

Dithiothreitol (DTT) is a thiol-reducing reagent that quantitatively reduces disulfide (SH) groups in biological molecules. It specifically targets 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 less toxic than 2-mercaptoethanol. Typically, a seven-fold lower concentration of DTT (100 mm) is more efficient than that of 2-mercaptoethanol (5% v/v, 700 mm).

Application

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).

DTT has been used:

as an enzyme stabilizer to maintain exebacase stability[1]
for peptide extraction and protein denaturation[2]
in sample preparation and reversal of formaldehyde crosslinks before mass spectrometry[3]
as a buffer component to extract synaptogliosome[4]

Biochem/physiol Actions

Dithiothreitol (DTT) is broadly used in chemical peptide synthesis and biochemical preparations of thiol proteins. Additionally, studies on protein folding and enzyme activity in protein chemistry make use of DTT. This reagent explicitly mediates the thiol-disulfide exchange reaction to completely reduce the intra-or between sub-atomic disulfide bonds in biomolecules. This reaction brings about the arrangement of thiols and the cyclic disulfide of DTT.[5]

Features and Benefits

BioUltra grade powder suitable for molecular biology
DNase, RNase, phosphatase, and protease-free insoluble matter, passes the filter test
Stringently tested and free from trace metals

Other Notes

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

Isolation of RNA using guanidinium salts. Inclusion of a reductant enhances denaturation by breaking intramolecular protein disulfide bonds.[6]

Pictograms

GHS05,GHS07

signalword

Danger

hcodes

H302,H315,H318

pcodes

P264 - P280 - P301 + P312 - P302 + P352 - P305 + P351 + P338 - P332 + P313

Hazard Classifications

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c