Tag: M.W=150-200

Diemer, Vincent team published research on Nature Communications in 2020 | 144-48-9

Application In Synthesis 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 everyday life, iodide is most commonly encountered as a component of iodized salt, which many governments mandate. 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide. Worldwide, iodine deficiency affects two billion people and is the leading preventable cause of intellectual disability. Application In Synthesis of 144-48-9.

Diemer, Vincent;Ollivier, Nathalie;Leclercq, Berenice;Drobecq, Herve;Vicogne, Jerome;Agouridas, Vangelis;Melnyk, Oleg research published 《 A cysteine selenosulfide redox switch for protein chemical synthesis》, the research content is summarized as follows. The control of cysteine reactivity is of paramount importance for the synthesis of proteins using the native chem. ligation (NCL) reaction. We report that this goal can be achieved in a traceless manner during ligation by appending a simple N-selenoethyl group to cysteine. While in synthetic organic chem. the cleavage of carbon-nitrogen bonds is notoriously difficult, we describe that N-selenoethyl cysteine (SetCys) loses its selenoethyl arm in water under mild conditions upon reduction of its selenosulfide bond. Detailed mechanistic investigations show that the cleavage of the selenoethyl arm proceeds through an anionic mechanism with assistance of the cysteine thiol group. The implementation of the SetCys unit in a process enabling the modular and straightforward assembly of linear or backbone cyclized polypeptides is illustrated by the synthesis of biol. active cyclic hepatocyte growth factor variants.

Application In Synthesis 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

Dorst, Andrea team published research on ACS Medicinal Chemistry Letters in 2020 | 144-48-9

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., Formula: C2H4INO

Iodide is one of the largest monatomic anions. It is assigned a radius of around 206 picometers. 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide.For comparison, the lighter halides are considerably smaller: bromide (196 pm), chloride (181 pm), and fluoride (133 pm). In part because of its size, iodide forms relatively weak bonds with most elements. Formula: C2H4INO.

Dorst, Andrea;Berg, Regina;Gertzen, Christoph G. W.;Schafle, Daniel;Zerbe, Katja;Gwerder, Myriam;Schnell, Simon D.;Sander, Peter;Gohlke, Holger;Gademann, Karl research published 《 Semisynthetic Analogs of the Antibiotic Fidaxomicin-Design, Synthesis, and Biological Evaluation》, the research content is summarized as follows. The glycosylated macrocyclic antibiotic fidaxomicin (tiacumicin B, lipiarmycin A3) displays good to excellent activity against Gram-pos. bacteria and was approved for the treatment of Clostridium difficile infections (CDI). Among the main limitations for this compound, its low water solubility impacts further clin. uses. We report on the synthesis of new fidaxomicin derivatives based on structural design and utilizing an operationally simple one-step protecting group-free preparative approach from the natural product. An increase in solubility of up to 25-fold with largely retained activity was observed Furthermore, hybrid antibiotics were prepared that show improved antibiotic activities.

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., Formula: C2H4INO

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

Eissa, Ibrahim H. team published research on Bioorganic Chemistry in 2021 | 144-48-9

HPLC of Formula: 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.

Iodide is one of the largest monatomic anions. It is assigned a radius of around 206 picometers. 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide.For comparison, the lighter halides are considerably smaller: bromide (196 pm), chloride (181 pm), and fluoride (133 pm). In part because of its size, iodide forms relatively weak bonds with most elements. HPLC of Formula: 144-48-9.

Eissa, Ibrahim H.;Dahab, Mohammed A.;Ibrahim, Mohamed K.;Alsaif, Nawaf A.;Alanazi, A. Z.;Eissa, Sally I.;Mehany, Ahmed B. M.;Beauchemin, Andre M. research published 《 Design and discovery of new antiproliferative 1,2,4-triazin-3(2H)-ones as tubulin polymerization inhibitors targeting colchicine binding site》, the research content is summarized as follows. Thirty-five new colchicine binding site inhibitors was designed and synthesized based on the 1,2,4-triazin-3(2H)-one nucleus I [n= 1, 2; R = NH2, OH, OEt; R1= R2= R3 = R4= H; R1= R2= R3 = R4 = OMe; R1= OMe, R2, R3, R4 = H, etc.]. Such mols. I were synthesized through a cascade reaction between readily accessible α-amino ketones and Ph carbazate as a masked N-isocyanate precursor. The synthesized derivatives I were cisoid restricted combretastatin A4 analogs containing 1,2,4-triazin-3(2H)-one in place of the olefinic bond, and they had the same essential pharmacophoric features of colchicine binding site inhibitors. The synthesized compounds I were evaluated in-vitro for their antiproliferative activities against a panel of three human cancer cell lines (MCF-7, HepG-2, and HCT-116), using colchicine as a pos. control. Among them, two compounds I [n= 2; R = OH; R1, R2 ,R4 = OMe, R3 = H] and I [n= 2; R = NH2; R1, R2 ,R4 = OMe, R3 = H] demonstrated a significant antiproliferative effect against all cell lines with IC50 ranging from 8.2 – 18.2μM. Further investigation was carried out for the most active cytotoxic agents as tubulin polymerization inhibitors. Compounds I [n= 2; R = OH; R1, R2 ,R4 = OMe, R3 = H] and I [n= 2; R = NH2; R1, R2 ,R4 = OMe, R3 = H] effectively inhibited microtubule assembly with IC50 values ranging from 3.9 to 7.8μM. Tubulin polymerization assay results were found to be comparable with the cytotoxicity results. The cell cycle anal. revealed significant G2/M cell cycle arrest of the analog I [n= 2; R = OH; R1, R2 ,R4 = OMe, R3 = H] in HepG-2 cells. The most active compounds I [n= 2; R = OEt; R1, R2 ,R4 = OMe, R3 = H], I [n= 2; R = OEt; R1, R2 ,R3 = R4 = OMe], I [n= 2; R = OH; R1= OMe, R2, R3, R4 = H], I [n= 2; R = OH; R1, R2, R4 = OMe, R3 = H] and I [n= 2; R = NH2; R1, R2 ,R4 = OMe, R3 = H] did not induce significant cell death in normal human lung cells Wl-38, suggesting their selectivity against cancer cells. Also, these compounds upregulated the level of active caspase-3 and boosted the levels of the pro-apoptotic protein Bax by five to seven folds in comparison to the control. Moreover, apoptosis analyses were conducted for compound I [n= 2; R = OH; R1, R2 ,R4 = OMe, R3 = H] evaluated its apoptotic potential. Finally, in-silico studies were conducted and revealed the probable interaction with the colchicine binding site. ADME prediction of the designed compounds I showed that they were not only with promising tubulin polymerization inhibitory activity but also with favorable pharmacokinetic and drug-likeness properties.

HPLC of Formula: 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

Elshafei, Ali M. team published research on Journal of Microbiology, Biotechnology and Food Sciences in 2021 | 144-48-9

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., Safety of 2-Iodoacetamide

Alkyl iodides react at a faster rate than alkyl fluorides due to the weak C-I bond. Iodo alkanes participate in a variety of organic synthesis reactions, which include the Simmons-Smith reaction (cyclopropanation using iodomethane), 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide. Williamson ether synthesis, Wittig reaction, Grignard reaction, alkyl coupling reactions, and Wurtz reaction. Safety of 2-Iodoacetamide.

Elshafei, Ali M.;El-Ghonemy, Dina H. research published 《 Extracellular glutaminase-free L-asparaginase from Trichoderma viride F2: purification, biochemical characterization and evaluation of its potential in mitigating acrylamide formation in starchy fried food》, the research content is summarized as follows. L-asparaginase is an antitumor agent that suppresses cancer cell growth by eliminating L-asparagine from malignant cells. However, the intrinsic glutaminase activity is responsible for significant life-threatening adverse effects. Therefore, glutaminase-free L-asparaginase is far required to improve the therapeutic efficacy of L-asparaginase treatment. L-asparaginase was also used to combat the development of acrylamide in foods rich in carbohydrates cooked at high temperatures Therefore, this study explores the purification and characterization of glutaminase-free L-asparaginase from Trichoderma viride F2 using agro-industrial residues as substrate. The enzyme was purified 36-folds with 688.1 U/mg specific activity and a final yield of 38.9% through ethanol precipitation, gel filtration on Sephadex G-100 followed by Sephadex G-200. The purified L-asparaginase is monomeric with a mol. mass of 57 kDa and exhibited optimum activity at pH 7.5 and 37 °C, which is relatively close to the human body′s internal environment. The purified L-asparaginase showed high affinity and catalytic efficiency towards its natural substrate L-asparagine with Km and Vmax of 1.2 mM and 71.3 U/mL, resp., and did not exhibit any intrinsic glutaminase activity. Among the salts tested, the univalent cations Na+ and K+ enhanced the activity by 145.7% and 163.5%, resp., while the presence of Ag+ and Fe+3 displayed a considerable loss in activity. The enzyme showed a good anti-oxidant activity with IC50 of 66.1μg/mL and was able to convert L-asparagine exist in potatoes to L-aspartic acid and ammonia, suggesting its use as anti-carcinogenic agent and as potential food industry candidate to mitigate acrylamide content in starchy fried food.

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., Safety of 2-Iodoacetamide

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

Espinosa, Luis Ariel team published research on Analytical and Bioanalytical Chemistry in 2021 | 144-48-9

Recommanded Product: 2-Iodoacetamide, 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.

Alkyl iodides react at a faster rate than alkyl fluorides due to the weak C-I bond. Iodo alkanes participate in a variety of organic synthesis reactions, which include the Simmons-Smith reaction (cyclopropanation using iodomethane), 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide. Williamson ether synthesis, Wittig reaction, Grignard reaction, alkyl coupling reactions, and Wurtz reaction. Recommanded Product: 2-Iodoacetamide.

Espinosa, Luis Ariel;Ramos, Yassel;Andujar, Ivan;Torres, Enso Onill;Cabrera, Gleysin;Martin, Alejandro;Roche, Diamile;Chinea, Glay;Becquet, Monica;Gonzalez, Isabel;Canaan-Haden, Camila;Nelson, Elias;Rojas, Gertrudis;Perez-Masson, Beatriz;Perez-Martinez, Dayana;Boggiano, Tamy;Palacio, Julio;Lozada Chang, Sum Lai;Hernandez, Lourdes;de la Luz Hernandez, Kathya Rashida;Markku, Saloheimo;Vitikainen, Marika;Valdes-Balbin, Yury;Santana-Medero, Darielys;Rivera, Daniel G.;Verez-Bencomo, Vicente;Emalfarb, Mark;Tchelet, Ronen;Guillen, Gerardo;Limonta, Miladys;Pimentel, Eulogio;Ayala, Marta;Besada, Vladimir;Gonzalez, Luis Javier research published 《 In-solution buffer-free digestion allows full-sequence coverage and complete characterization of post-translational modifications of the receptor-binding domain of SARS-CoV-2 in a single ESI-MS spectrum》, the research content is summarized as follows. Subunit vaccines based on the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 provide one of the most promising strategies to fight the COVID-19 pandemic. The detailed characterization of the protein primary structure by mass spectrometry (MS) is mandatory, as described in ICHQ6B guidelines. In this work, several recombinant RBD proteins produced in five expression systems were characterized using a non-conventional protocol known as in-solution buffer-free digestion (BFD). In a single ESI-MS spectrum, BFD allowed very high sequence coverage (≥ 99%) and the detection of highly hydrophilic regions, including very short and hydrophilic peptides (2-8 amino acids), and the His6-tagged C-terminal peptide carrying several post-translational modifications at Cys538 such as cysteinylation, homocysteinylation, glutathionylation, truncated glutathionylation, and cyanylation, among others. The anal. using the conventional digestion protocol allowed lower sequence coverage (80-90%) and did not detect peptides carrying most of the above-mentioned PTMs. The two C-terminal peptides of a dimer [RBD(319-541)-(His)6]2 linked by an intermol. disulfide bond (Cys538-Cys538) with twelve histidine residues were only detected by BFD. This protocol allows the detection of the four disulfide bonds present in the native RBD, low-abundance scrambling variants, free cysteine residues, O-glycoforms, and incomplete processing of the N-terminal end, if present. Artifacts generated by the in-solution BFD protocol were also characterized. BFD can be easily implemented; it has been applied to the characterization of the active pharmaceutical ingredient of two RBD-based vaccines, and we foresee that it can be also helpful to the characterization of mutated RBDs.

Recommanded Product: 2-Iodoacetamide, 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

Fu, Lingxiao team published research on Chemosphere in 2021 | 144-48-9

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., Recommanded Product: 2-Iodoacetamide

Iodide is one of the largest monatomic anions. It is assigned a radius of around 206 picometers. 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide.For comparison, the lighter halides are considerably smaller: bromide (196 pm), chloride (181 pm), and fluoride (133 pm). In part because of its size, iodide forms relatively weak bonds with most elements. Recommanded Product: 2-Iodoacetamide.

Fu, Lingxiao;Wu, Xiaofeng;Zhu, Yongbin;Yao, Lei;Wu, Chengqiang;Cheng, Haixiang;Xu, Yiran;Hu, Jun;Gao, Weijun research published 《 Iodinated disinfection byproduct formation in a MnO2/I–/EPS system》, the research content is summarized as follows. Manganese dioxide (MnO2) is a Mn deposit widely accumulated in the corrosion layer of pipelines, and iodide (I-) is a halogen ion frequently detected in waters. The biofilm dwelling on the corrosion scales often secretes extracellular polymeric substances (EPS) into drinking water. The paper aimed to study the I- oxidation by MnO2 and iodinated disinfection byproducts (I-DBPs) formation with biofilm EPS as a precursor. More than 93% of formed free iodine was finally converted into organic iodine in the MnO2/I-/EPS system. Compared with humic acid, EPS had a lower carbonaceous I-DBPs (C-IDBPs) formation while a higher nitrogenous I-DBPs (N-IDBPs) formation. The formation of iodomethanes (I-THMs), iodoacetonitriles (I-HANs) and iodoacetic acids (I-HAAs) decreased with the increase of pH due to the weakening of polarization effect and redox potential, while the iodoacetamides (I-HAcAms) formation achieved the maximum at pH 6.0 due to the difference between the hydrolysis rate of I-HANs and decomposition rate of I-HAcAms. The I-DBPs formation was pos. correlated with I- concentration, while neg. correlated with MnO2 dose. Protein components displayed a higher formation of N-IDBPs and C-IDBPs than polysaccharide components due to higher nitrogen proportion and more iodination sites. Among 20 protein monomers, aspartic acid was considered as the most important precursor of the four investigated I-DBPs species. The paper is helpful to understand the I-DBPs formation when I- in the bulk water come into contact with Mn deposits attached by biofilm.

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., Recommanded Product: 2-Iodoacetamide

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

den Ridder, Maxime team published research on Journal of Proteomics in 2022 | 144-48-9

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., HPLC of Formula: 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. HPLC of Formula: 144-48-9.

den Ridder, Maxime;Knibbe, Ewout;van den Brandeler, Wiebeke;Daran-Lapujade, Pascale;Pabst, Martin research published 《 A systematic evaluation of yeast sample preparation protocols for spectral identifications, proteome coverage and post-isolation modifications》, the research content is summarized as follows. The importance of obtaining comprehensive and accurate information from cellular proteomics experiments asks for a systematic investigation of sample preparation protocols. In particular when working with unicellular organisms with strong cell walls, such as found in the model organism and cell factory Saccharomyces cerevisiae. Here, we performed a systematic comparison of sample preparation protocols using a matrix of different conditions commonly applied in whole cell lysate, bottom-up proteomics experiments The different protocols were evaluated for their overall fraction of identified spectra, proteome and amino acid sequence coverage, GO-term distribution and number of peptide modifications, by employing a combination of database and unrestricted modification search approaches. Ultimately, the best protocols enabled the identification of approx. 65-70% of all acquired fragmentation spectra, where addnl. de novo sequencing suggests that unidentified spectra were largely of too low spectral quality to provide confident spectrum matches. Generally, a range of peptide modifications could be linked to solvents, additives as well as filter materials. Most importantly, the use of moderate incubation temperatures and times circumvented excessive formation of modification artifacts. The collected protocols and large sets of mass spectrometric raw data provide a resource to evaluate and design new protocols and guide the anal. of (native) peptide modifications. The single-celled eukaryote yeast is a widely used model organism for higher eukaryotes in which, for example, the regulation of glycolysis is studied in the context of health and disease. Moreover, yeast is a widely employed cell factory because it is one of the few eukaryotic organisms that can efficiently grow under both aerobic and anaerobic conditions. Large-scale proteomics studies have become increasingly important for single-celled model organisms, such as yeast, in order to provide fundamental understanding of their metabolic processes and proteome dynamics under changing environmental conditions. However, comprehensive and accurate cellular proteomics experiments require optimized sample preparation procedures, in particular when working with unicellular organisms with rigid cell walls, such as found in yeast. Protocols may substantially bias towards specific protein fractions, modify native protein modifications or introduce artificial modifications. That lowers the overall number of spectral identifications and challenges the study of native protein modifications. Therefore, we performed a systematic study of a large array of protocols on yeast grown under highly controlled conditions. The obtained outcomes, the collected protocols and the mass spectrometric raw data enable the selection of suitable sample preparation elements and furthermore support the evaluation of (native) peptide modifications in yeast, and beyond.

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., HPLC of Formula: 144-48-9

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

Davis, Lissa A. team published research on Physiology & Behavior in 2021 | 144-48-9

SDS of cas: 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.

Organic iodides are used in veterinary products (Organic Iodide Powder) as a nutritional source of iodine. 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide. In the chemical industry, alkyl iodides serve as excellent alkylating agents and, specifically, methyl iodide is used as a methylating agent in the synthesis of various pharmaceutical drugs. SDS of cas: 144-48-9.

Davis, Lissa A.;Running, Cordelia A. research published 《 Repeated exposure to epigallocatechin gallate solution or water alters bitterness intensity and salivary protein profile》, the research content is summarized as follows. Polyphenols, bitter and astringent compounds present in many healthy foods, induce varied sensory responses across individuals. These differences in liking and flavor intensity may be attributable, in part, to differences in saliva. In the current study, we tested the effect of repeated consumption of a bitter polyphenol (epigallocatechin gallate, EGCG) solution on perceived bitterness intensity and salivary protein composition We hypothesized exposure to EGCG would cause an increase in concentrations of salivary proteins that inhibit bitterness of polyphenols. We also hypothesized that participants with higher habitual polyphenol, specifically the flavanols, intake would experience less bitterness from EGCG solutions than those with low habitual intake, and that the high flavanol consumers would be more resistant to salivary alterations. We also tested whether bovine milk casein, a food analog for salivary proteins that may suppress bitterness, would decrease bitterness intensity of the EGCG solution and mitigate effects of the intervention. Participants (N = 37) in our crossover intervention adhered to two-week periods of daily bitter (EGCG) or control (water) solution consumption. Bitterness intensity ratings and citric acid-stimulated saliva were collected at baseline and after each exposure period. Results indicate that bitterness intensity of the EGCG solution decreased after polyphenol (bitter EGCG) exposure compared to control (water) exposure. Casein addition also decreased bitterness intensity of the EGCG solution While there was not a significant overall main effect of baseline flavanol intake on solution bitterness, there was an interaction between intervention week and baseline flavanol intake. Surprisingly, the higher flavanol intake group rated EGCG solutions as more bitter than the low and medium intake groups. Of proteins relevant to taste perception, several cystatins changed in saliva in response to the intervention. Interestingly, most of these protein alterations occurred more robustly after the control (water) exposure rather than the bitter (EGCG) exposure, suggesting that addnl. factors not quantified in this work may influence salivary proteins. Thus, we confirm in this study that exposure to bitterness suppresses ratings of bitterness over time, but more work needs to establish the causal factors of how diet influences salivary proteins.

SDS of cas: 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

Dahdouh, Amel team published research on Biocatalysis and Biotransformation in | 144-48-9

Application In Synthesis 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.

Organic iodides are used in veterinary products (Organic Iodide Powder) as a nutritional source of iodine. 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide. In the chemical industry, alkyl iodides serve as excellent alkylating agents and, specifically, methyl iodide is used as a methylating agent in the synthesis of various pharmaceutical drugs. Application In Synthesis of 144-48-9.

Dahdouh, Amel;Boucherba, Nawel;Bouacem, Khelifa;Mechri, Sondes;Amirouche, Adel;Aksas, Ali;Jaouadi, Bassem;Kati, Djamel Edine research published 《 A new peroxidase from the roots of the Algerian white turnip (Brassica rapa, variety rapa): extraction, purification, characterisation, and antioxidant potential》, the research content is summarized as follows. Due to its various biol. activities, the roots of Brassica rapa (turnip), has been applied as a therapeutic agent in traditional medicine. The current study aimed to purify a plant peroxidase (POD; designated as TRP) from Algerian white turnip (B. rapa, variety rapa) roots, to homogeneity and to characterize it biochem. The mol. weight of the purified TRP was determined to be ∼58 kDa as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and high-performance liquid chromatog. (HPLC). The TRP Reinheitzahl values (RZ) and specific activity were 2.9 and 14,500 U/mg, resp. Its N-terminal sequence exhibited high identity with those of class III-PODs. TRP showed optimal activity at 55 °C and pH 6 (guaiacol), was completely inhibited by sodium azide (NaN3) and potassium cyanide (KCN) and exhibited greater catalytic efficiency than that of the well-known horseradish peroxidase (HRP) from Armoracia rusticana. TRP demonstrated antioxidant activities with 45% and 61.49% of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS•) and hydroxyl (•OH) radical scavenging, resp., as well as ferrous ion chelating (52.96%) and reducing (48.32%) powers. This study provides information regarding the potential role of TRP in enzyme therapy (as applied in the pharmaceutical and medicinal industries), with biol. eradication of free radicals.

Application In Synthesis 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

da Silva-Lopez, Raquel Elisa team published research on Brazilian Journal of Microbiology in | 144-48-9

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., COA of Formula: C2H4INO

Iodide is one of the largest monatomic anions. It is assigned a radius of around 206 picometers. 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide.For comparison, the lighter halides are considerably smaller: bromide (196 pm), chloride (181 pm), and fluoride (133 pm). In part because of its size, iodide forms relatively weak bonds with most elements. COA of Formula: C2H4INO.

da Silva-Lopez, Raquel Elisa;de Araujo, Thayane Aparecida Alves;Monteiro, Helvio Jose Jalles;Teixeira, Erika Maria Gomes Ferreira;Tupi, Lucas;da Silva Bon, Elba Pinto research published 《 Study of protease activity from Aspergillus awamori INCQS2B.361U2/1 extracellular fraction and modification of culture medium composition to isolate a novel aspartic protease》, the research content is summarized as follows. Aspergillus awamori was cultivated in a modified Breccia medium, and the extracellular fraction was obtained, which presented 260 ±15μg of protein/mg and specific protease activity of 3.87 ± 0.52 mM.min-1.mg of protein-1using Nα-p-tosyl-L-arginine Me ester hydrochloride (L-TAME) as substrate. This fraction showed major proteins about 104 and 44 kDa and maximal protease activity at pH 5.5, 6.5, and 9.0, suggesting that A. awamori secretes acidic, neutral, and alk. proteases with expressive thermal stability, however, aspartic protease was the most important activity. When yeast extract was supplemented to a modified Breccia medium, A. awamori protein secretion and protease activity were maximal and the affinity chromatog. on pepstatin-agarose was employed to isolate the aspartic protease activity, which was called ASPA, with approx. 75 kDa. ASPA maximal activity was obtained at pH 4.5 and 6.5, and 50 °C. Pepstatin inhibited about 80% of ASPA activity, with IC50 and Ki values of 0.154 and 0.072 μM, resp. ASPA cleaved protein and peptides substrates with the highest activity against gelatin (95 U/mg) and good peptidase activity with KM 0.0589 mM and Vmax 1.909 mM.min-1.mg protein-1, using L-TAME as substrate. A. awamori extracellular fraction is a source of proteases with important activity, and the supplementation of modified Breccia medium increased the aspartic protease production This enzyme presented different biochem. characteristics from the previously reported A. awamori aspartic proteases. Therefore, ASPA is an excellent candidate for biotechnol. application due to its important activity and thermostability.

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., COA of Formula: C2H4INO

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