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In vitro transcription of capped mRNA with modified nucleotides and Poly(A) tail
TSA (Tyramide Signal Amplification), used for signal amplification of ISH, IHC and IC etc.
Separation of phosphorylated and non-phosphorylated proteins without phospho-specific antibody
A convenient and sensitive way for cell proliferation assay and cytotoxicity assay
Protect the integrity of proteins from multiple proteases and phosphatases for different applications.
DL-Dithiothreitol is capable of maintaining monothiols completely in the reduced state and of reducing disulfides quantitatively. Thiol groups such as those of coenzyme A are readily oxidized in air to disulfides. To maintain these groups in the reduced state, another thiol is often added so that interchange takes place. Since DL-dithiothreitol is a highly alcohol- and water-soluble solid with little odor and little tendency to be oxidized directly by air, it proves much superior to the thiols currently used as protective reagents for sulfhydryl groups. DL-Dithiothreitol is commonly used in a variety of experiments that involve peptides or proteins, protecting sulfhydryl groups from oxidation and reducing disulfide bonds between cysteines. DL-Dithiothreitol also acts as an "antidote" enabling the activity of detoxification systems, and is used in the treatment approach of diseases like cystinosis or medical conditions resulting from ion or metal toxicity.
References:
1. Cleland WW. Dithiothreitol, a new protective reagent for SH groups. Biochemistry, 1964, 3: 480-482.
2. Lopes de Almeida JP, Saldanha C. Dithiothreitol revisited in red cells: a new head for an old hat. Clinical Hemorheology and Microcirculation, 2010, 46(1): 51-56.