Chelating & Reducing Agents

Image shows redox chemical reaction

Figure 1.Redox chemical reaction: An oxidation-reduction reaction occurs when a reducing agent (A) and oxidizing agent (B) are combined. In this process, Compound A loses electrons (oxidation) to compound B (reduction).

Reducing agents, also known as reducers or reductants, are essential for studying protein in biochemistry1 and are used in various techniques in proteomics, such as protein denaturation and solubilization. They are especially useful in stabilizing free sulfhydryl groups and reducing disulfide bonds of proteins and peptides2. These reducers donate electrons in a redox chemical reaction (Figure 1). Reagents, such as dithiothreitol (DTT) also called Cleland’s reagent, dithioerythritol (DTE), tris(2-carboxyethyl)phosphine (TCEP), β-mercaptoethanol (BME), sodium dithionate, and nitrilotriacetic acid (NTA) are used widely as noble-reducing agents. 

Image shows example of EDTA chelating metal ion in the blood stream

Figure 2.Example of Ethylenediaminetetraacetic acid (EDTA) chelating metal ion in the blood stream to remove plaque from an artery.

Chelators, or chelating agents, remove heavy metals3 by binding to metal ions to form two or more bonds with their ring-like structure to build a water-soluble, stable structure. Common chelating agents include ethylenediaminetetraacetic acid (EDTA), ethylene glycol tetraacetic acid (EGTA) and ethylenediamine (Figure 2). Research has demonstrated that using chelating reagents, in combination with reducing reagents, supports in the removal of cationic heavy metals as well as anionic contaminants, such as arsenic4.

Choose from our comprehensive range of reducing and chelating agents, available in various high purities and forms, such as liquid, solution, crystalline solid, and powder, for your scientific advancement.


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Getz EB, Xiao M, Chakrabarty T, Cooke R, Selvin PR. 1999. A Comparison between the Sulfhydryl Reductants Tris(2-carboxyethyl)phosphine and Dithiothreitol for Use in Protein Biochemistry. Analytical Biochemistry. 273(1):73-80.
Wedemeyer WJ, Welker E, Narayan M, Scheraga HA. 2000. Disulfide Bonds and Protein Folding. Biochemistry. 39(15):4207-4216.
Amadi CN, Offor SJ, Frazzoli C, Orisakwe OE. 2019. Natural antidotes and management of metal toxicity. Environ Sci Pollut Res. 26(18):18032-18052.
Kim EJ, Jeon E, Baek K. 2016. Role of reducing agent in extraction of arsenic and heavy metals from soils by use of EDTA. Chemosphere. 152274-283.
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