Wu, Shang-Chuen team published research in Methods in molecular biology (Clifton, N.J.) in 2022 | 144-48-9

Electric Literature of 144-48-9, 2-Iodoacetamide is a synthetic retinoid that binds to the DNA of cells, altering transcription. It also has been found to be effective in treating bowel disease and has been shown to have dna binding activity. The compound was synthesized by attaching iodine molecules to acetamide. 2-Iodoacetamide targets the protein thiols on the surface of cells, which are responsible for oxidation and damage due to reactive oxygen species (ROS). This compound is metabolized by alcohol dehydrogenase and can be used as a biological sample or natural compound is a compound used as an electrophile for covalent modification of nucleophilic residues on proteins (cysteine, methionine, histidine). When modifying the active-site residues of cysteine proteases, α-Iodoacetamide acts as an irreversible inhibitor of these enzymes.

2-Iodoacetamide used in peptide mapping because it covalently binds with thiols in cysteine residues, thereby preventing disulfide bond formation. By virtue of reaction with cysteine, it is an irreversible inhibitor of enzymes with cysteine at the active site. Also reacts with histidine residues though much more slowly, and this activity is responsible for inhibition of ribonuclease.
An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate., 144-48-9.

In general, organic iodides are light-sensitive and turn yellow during storage, owing to the formation of iodine. 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide.Organic iodides can be alkyl, alkenyl, or alkynyl, and all of them are very reactive toward with many kinds of nucleophiles. Electric Literature of 144-48-9.

Wu, Shang-Chuen;Paul, Anu;Cummings, Richard D;Feasley, Christa L;Arthur, Connie M;Stowell, Sean R research published 《 Alkylation of Galectin-1 with Iodoacetamide and Mass Spectrometric Mapping of the Sites of Incorporation.》, the research content is summarized as follows. Galectins can display unique sensitivity to oxidative changes that result in significant conformational alterations that prevent carbohydrate recognition. While a variety of approaches can be utilized to prevent galectin oxidation, several of these require inclusion of reducing agents that not only prevent galectins from undergoing oxidative inactivation but can also interfere with normal redox potentials required for fundamental cellular processes. To overcome the limitations associated with placing cells in an artificial reducing environment, cysteine residues on galectins can be directly alkylated with iodoacetamide to form a stable thioether adduct that is resistant to further modification. Iodoacetamide alkylated galectin remains stable over prolonged periods of time and retains the carbohydrate binding and biological activities of the protein. As a result, this approach allows examination of the biological roles of a stabilized form of galectin-1 without introducing the confounding variables that can occur when typical soluble reducing agents are employed.

Electric Literature of 144-48-9, 2-Iodoacetamide is a synthetic retinoid that binds to the DNA of cells, altering transcription. It also has been found to be effective in treating bowel disease and has been shown to have dna binding activity. The compound was synthesized by attaching iodine molecules to acetamide. 2-Iodoacetamide targets the protein thiols on the surface of cells, which are responsible for oxidation and damage due to reactive oxygen species (ROS). This compound is metabolized by alcohol dehydrogenase and can be used as a biological sample or natural compound is a compound used as an electrophile for covalent modification of nucleophilic residues on proteins (cysteine, methionine, histidine). When modifying the active-site residues of cysteine proteases, α-Iodoacetamide acts as an irreversible inhibitor of these enzymes.

2-Iodoacetamide used in peptide mapping because it covalently binds with thiols in cysteine residues, thereby preventing disulfide bond formation. By virtue of reaction with cysteine, it is an irreversible inhibitor of enzymes with cysteine at the active site. Also reacts with histidine residues though much more slowly, and this activity is responsible for inhibition of ribonuclease.
An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate., 144-48-9.

Referemce:
Iodide – Wikipedia,
Iodide – an overview | ScienceDirect Topics – ScienceDirect.com