High Purity DL-Dithiothreitol CAS 3483-12-3

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DL-Dithiothreitol
3483-12-3

Name: DL-Dithiothreitol

Cas: 3483-12-3

Purity: 99%min

MOQ: 1KG

Directory Guidance on DL-Dithiothreitol

Chemical Structure

DL-Dithiothreitol
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Basic Info:

CAS No:3483-12-3
Formula:C4H10O2S2
EINECS:222-468-7
Stock AvailabilityIn stock
Brand NameLook chem
OriginChina

Product Introduction:

DL-Dithiothreitol (described as DTT) is a little molecule organic lowering representative with the chemical formula C4H10O2S2.

DL-Dithiothreitol is a frequently used decreasing representative with solid reducibility, which is mostly because of the conformational stability of the six-membered ring (consisting of disulfide bonds) in its oxidation state.

The isomer of Dithiothreitol is dithioerythritol (DTE), the C3-epimer of DTT.

The lowering power is influenced by the pH value, as well as it can just play a minimizing effect when the pH value is higher than 7.

Because of the low nucleophilicity of protonated sulfur, as the pH value lowers, the efficient reducibility of DTT additionally lowers.

Tris(2-carboxyethyl)phosphine hydrochloride (TCEP hydrochloride) can be made use of as a substitute for DL-Dithiothreitol under reduced pH conditions, and it is additionally more secure than DTT.

This is due to the fact that only the deprotonated thiolate anions (-S–) are responsive, while mercaptans (-SH) do not; and also the pKa of sulfhydryl teams is typically ~ 8.3.

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Product Usage:

DL-Dithiothreitol is utilized as reducing agent and deprotecting agent

  • One of making uses of DTT is as a decreasing agent and also deprotecting representative for sulfhydryl DNA.
  • Sulfhydryl DNA incurable sulfur atoms tend to form dimers in solution, specifically in the existence of oxygen.
  • This dimerization significantly lowers the efficiency of some combining response experiments (such as the immobilization of DNA in a biosensor).
  • Including DL-Dithiothreitol to the DNA option and also removing it after a period of response can reduce the dimerization of DNA.
  • DTT is also frequently utilized for the reduction of disulfide bonds in proteins, and can be utilized to prevent intermolecular or intramolecular disulfide bonds created in between cysteines in healthy proteins.
  • DL-Dithiothreitol is often incapable to reduce the disulfide bonds embedded in the protein framework (solvent inaccessible). The decrease of such disulfide bonds often requires denaturation of the healthy protein (home heating at heat or adding denaturing representatives, such as 6M guanidine hydrochloride, 8M Urea or 1% SDS).
  • As a matter of fact, according to the different decrease speed of disulfide bonds in the presence of DTT, the degree of embedding can be judged.
  • DTT can also be used to minimize the disulfide bridge of the crosslinking representative N, N’- bis( acryloyl) cystamine to break down the polyacrylamide gel matrix.

DTT can additionally be made use of as an oxidant

  • Compared to various other reagents such as glutathione, its major advantage is that there is really no mixed disulfide varieties.
  • In uncommon cases, DTT adducts might be created, that is, 2 sulfur atoms of DTT might form disulfide bonds with different sulfur atoms.
  • In this case, DL-Dithiothreitol cannot be cyclized because it has no remaining free thiol.

Applications in other areas:

  • Studies have shown the effect of dithiothreitol on the formation of lactoglobulin amyloid fibers. Amyloid fibers are related to human diseases such as Alzheimer’s disease, Parkinson’s disease and non-neural tissue amyloidosis.
  • The effects of reducing agent dithiothreitol on the formation of lactoglobulin amyloid fibers were studied by using ThT fluorescence, Congo red combination and transmission electron microscopy.
  • Therefore, disulfide bonds play a very critical role in the formation of lactoglobulin amyloid fibers.
  • In protein sequence analysis, it is used to remove disulfide linkages.
  • DL-Dithiothreitol is a protein that is often used to reduce disulfide bonds, more generally, to prevent intramolecular and intermolecular disulfide bonds from forming cysteine ​​residues in proteins.

Related References:

  1. Introduction: Encyclopedia of Chemicals, Drugs and Biological Products-O’Neil, Maryadele J | archive.
  2. Functional description of DL-Dithiothreitol-Journal of the American Chemical Society | 2012 Mar 7.
  3. Wikipedia
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