COA of Formula: C2H4INO, 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.
Organic iodides are organic compounds containing a carbon-iodine (C-I) bond. 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide.The carbon-iodine bond is weaker than other carbon-halogen bonds due to the poor electronegative nature of the iodine atom. COA of Formula: C2H4INO.
Young, K. Z.;Cartee, N. M. P.;Lee, S. J.;Keep, S. G.;Ivanova, M. I.;Wang, Michael M. research published 《 Electrophilic and Drug-Induced Stimulation of NOTCH3 N-terminal Fragment Oligomerization in Cerebrovascular Pathology》, the research content is summarized as follows. In vitro, NTF is capable of both spontaneous and catecholamine-enhanced cysteine-mediated oligomerization. Despite well-characterized genetic influence on CADASIL, environmental effects, including medication usage, on disease remain unclear. We studied effects of assorted electrophilic compounds and drugs on NTF oligomerization by SDS-PAGE and dynamic light scattering. We then examined direct proton pump inhibitor-NTF binding with antibodies designed against proton pump inhibitor-labeled proteins and mass spectrometry. Finally, we used monoclonal NTF antibodies with Proximity Ligation Assay to identify NTF oligomers in 3 CADASIL and 2 age-matched control brains. We identified enhancement of NTF oligomerization by two electrophilic cysteine-modifying compounds, N-ethylmaleimide and iodoacetamide, and an electrophilic compound capable of oxidizing cysteines, ferric chloride. Electrophilic clin. drugs (fenoldopam, omeprazole, tenatoprazole, lansoprazole, and rabeprazole) also promoted oligomerization, and we identified direct omeprazole-NTF and tenatoprazole-NTF complexes. Addnl., we provide novel evidence of NTF multimers in human CADASIL brains. A broad array of electrophilic chems., including clin. relevant drugs, influences oligomerization of a pathol. CADASIL protein, providing mechanistic insight into disease protein oligomerization. We posit that environmental influences, which may include usage of electrophilic drugs, may affect CADASIL presentations.
COA of Formula: C2H4INO, 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