Tag: M.W=150-200

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. Product Details of C2H4INO.

Itsumi, Momoe;Shiota, Masaki;Kajioka, Shunichi;Eto, Masatoshi research published 《 Profile of androgen receptor activators identified using high-throughput screen》, the research content is summarized as follows. In this study using distinct system, effectors on dopamine signalling were identified as candidates that prominently increase AR activity. Then, this study suggested novel function on AR signalling in several compounds, which may be useful or harmful in organs where AR signalling play a role. In conclusion, various candidates for AR activation were identified using high-throughput screening.

Product Details of 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

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. Formula: C2H4INO.

Hifumi, Emi;Taguchi, Hiroaki;Nonaka, Tamami;Harada, Takunori;Uda, Taizo research published 《 Finding and characterizing a catalytic antibody light chain, H34, capable of degrading the PD-1 molecule》, the research content is summarized as follows. Programmed cell death 1 (PD-1) is an immune checkpoint mol. regulating T-cell function. Preventing PD-1 binding to its ligand PD-L1 has emerged as an important tool in immunotherapy. Here, we describe a unique human catalytic antibody light chain, H34, which mediates enzymic degradation of human PD-1 peptides and recombinant human PD-1 protein and thus functions to prevent the binding of PD-1 with PD-L1. H34 degraded one half of the PD-1 mols. within about 6 h under the exptl. conditions. Investigating the acquisition of the catalytic function by H34, which belongs to subgroup I and lacks a Pro⁹⁵ residue in CDR-3, revealed the importance of this sequence, as a Pro⁹⁵-reconstituted mutant (H34-Pro⁹⁵(+)) exhibited very little catalytic activity to cleave PD-1. Interestingly, EDTA inhibited the catalytic activity of H34, which could work as a metallo-protease. Zn²⁺ or Co²⁺ ions may work as a cofactor. It is meaningfull that H34 was obtained from the human antibody gene taken from a healthy volunteer, suggesting that we potentially have such unique mols. in our body.

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

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. Electric Literature of 144-48-9.

Habgood, Matthew;Seiferth, David;Zaki, Afroditi-Maria;Alibay, Irfan;Biggin, Philip C. research published 《 Atomistic mechanisms of human TRPA1 activation by electrophile irritants through molecular dynamics simulation and mutual information analysis》, the research content is summarized as follows. The ion channel TRPA1 is a promiscuous chemosensor, with reported response to a wide spectrum of noxious electrophilic irritants, as well as cold, heat, and mechanosensation. It is also implicated in the inception of itch and pain and has hence been investigated as a drug target for novel analgesics. The mechanism of electrophilic activation for TRPA1 is therefore of broad interest. TRPA1 structures with the pore in both open and closed states have recently been published as well as covalent binding modes for electrophile agonists. However, the detailed mechanism of coupling between electrophile binding sites and the pore remains speculative. In addition, while two different cysteine residues (C621 and C665) have been identified as critical for electrophile bonding and activation, the bound geometry has only been resolved at C621. Here, we use mol. dynamics simulations of TRPA1 in both pore-open and pore-closed states to explore the allosteric link between the electrophile binding sites and pore stability. Our simulations reveal that an open pore is structurally stable in the presence of open pockets in the C621/C665 region, but rapidly collapses and closes when these pockets are shut. Binding of electrophiles at either C621 or C665 provides stabilization of the pore-open state, but mols. bound at C665 are shown to be able to rotate in and out of the pocket, allowing for immediate stabilization of transient open states. Finally, mutual information anal. of trajectories reveals an informational path linking the electrophile binding site pocket to the pore via the voltage-sensing-like domain, giving a detailed insight into the how the pore is stabilized in the open state.

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., Electric Literature of 144-48-9

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

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. Reference of 144-48-9.

Hall, David Ross;Yeung, Kirsten;Peng, Hui research published 《 Monohaloacetic Acids and Monohaloacetamides Attack Distinct Cellular Proteome Thiols》, the research content is summarized as follows. Disinfection byproduct (DBP) exposure has been linked to multiple adverse health outcomes. However, the mol. initiating events by which DBPs induce their toxicities remain unclear. Herein, we combined reporter cell lines and activity-based protein profiling (ABPP) chem. proteomics to identify the protein targets of three monohaloacetic acids (mHAAs) and three monohaloacetamides (mHAMs), at the proteome-wide level. While mHAAs and mHAMs have similar potencies in reducing MTT activity, mHAMs induced greater Nrf2-mediated oxidative stress responses, demonstrating their distinct toxicity pathways. ABPP on crude cell lysates suggested that general proteome thiol reactivity correlates with cytotoxicity. Interestingly, live cell ABPP results revealed class-specific proteins attacked by mHAMs or mHAAs. Subsequent proteomic anal. identified >100 unique targets per DBP. mHAMs preferentially react with redox proteins including disulfide oxidoreductase enzymes, accounting for their stronger Nrf2 responses. To further probe alkylation mechanisms, we directly monitored protein adducts and identified 120 and 37 unique peptides with iodoacetamide and iodoacetic acid adducts, resp. Of the latter, we confirmed glyceraldehyde-3-phosphate dehydrogenase as a key target of IAA, specifically attacking the catalytic Cys 152. This is the first study reporting the distinct cellular protein targets of mHAAs and mHAMs at the proteome-wide level, which highlights their different toxicity pathways despite their similar structures.

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., Reference of 144-48-9

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

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. Formula: C2H4INO.

Hepworth, Christopher;Wood, William H. J.;Emrich-Mills, Tom Z.;Proctor, Matthew S.;Casson, Stuart;Johnson, Matthew P. research published 《 Dynamic thylakoid stacking and state transitions work synergistically to avoid acceptor-side limitation of photosystem I》, the research content is summarized as follows. TAP38/STN7-dependent (de)phosphorylation of light-harvesting complex II (LHCII) regulates the relative excitation rates of photosystems I and II (PSI, PSII) (state transitions) and the size of the thylakoid grana stacks (dynamic thylakoid stacking). Yet, it remains unclear how changing grana size benefits photosynthesis and whether these two regulatory mechanisms function independently. Here, by comparing Arabidopsis wild-type, stn7 and tap38 plants with the psal mutant, which undergoes dynamic thylakoid stacking but lacks state transitions, we explain their distinct roles. Under low light, smaller grana increase the rate of PSI reduction and photosynthesis by reducing the diffusion distance for plastoquinol; however, this beneficial effect is only apparent when PSI/PSII excitation balance is maintained by state transitions or far-red light. Under high light, the larger grana slow plastoquinol diffusion and lower the equilibrium constant between plastocyanin and PSI, maximizing photosynthesis by avoiding PSI photoinhibition. Loss of state transitions in low light or maintenance of smaller grana in high light also both bring about a decrease in cyclic electron transfer and over-reduction of the PSI acceptor side. These results demonstrate that state transitions and dynamic thylakoid stacking work synergistically to regulate photosynthesis in variable light.

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

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. Reference of 144-48-9.

Hamitouche, Fella;Armengaud, Jean;Dedieu, Luc;Duport, Catherine research published 《 Cysteine Proteome Reveals Response to Endogenous Oxidative Stress in Bacillus cereus》, the research content is summarized as follows. At the end of exponential growth, aerobic bacteria have to cope with the accumulation of endogenous reactive oxygen species (ROS). One of the main targets of these ROS is cysteine residues in proteins. This study uses liquid chromatog. coupled to high-resolution tandem mass spectrometry to detect significant changes in protein abundance and thiol status for cysteine-containing proteins from Bacillus cereus during aerobic exponential growth. The proteomic profiles of cultures at early-, middle-, and late-exponential growth phases reveals that (i) enrichment in proteins dedicated to fighting ROS as growth progressed, (ii) a decrease in both overall proteome cysteine content and thiol proteome redox status, and (iii) changes to the reduced thiol status of some key proteins, such as the transition state transcriptional regulator AbrB. Taken together, our data indicate that growth under oxic conditions requires increased allocation of protein resources to attenuate the neg. effects of ROS. Our data also provide a strong basis to understand the response mechanisms used by B. cereus to deal with endogenous oxidative stress.

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., Reference of 144-48-9

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

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. Category: iodides-buliding-blocks.

Grassi, Bruno;Hogan, Michael C.;Gladden, L. Bruce research published 《 Microvascular O₂ delivery and O₂ utilization during metabolic transitions in skeletal muscle. One-hundred years after the pioneering work by August Krogh》, the research content is summarized as follows. A review. Upon a sudden rise in work rate, ATP turnover increases immediately, whereas the adjustment of ATP resynthesis from oxidative phosphorylation is substantially slower. An “O₂ deficit” (energy borrowed from substrate level phosphorylation) is therefore generated. A greater O₂ deficit represents an epiphenomenon of a lower “metabolic stability” during the transition, a circumstance directly related to impaired exercise tolerance. In the search for factors responsible for the delayed adjustment of oxidative phosphorylation, we performed studies in the surgically isolated canine gastrocnemius muscle in situ. Enhancement of convective and diffusive microvascular O₂ delivery, with respect to a “normal” condition, did not affect skeletal muscle VO₂ kinetics during transitions to submaximal metabolic rates. VO₂ kinetics, however, was slowed after exptl. impairing convective O₂ delivery, a condition frequently encountered in pathol. conditions. Among potential metabolic factors (pyruvate dehydrogenase activation, nitric oxide inhibition of cytochrome oxidase) a limiting role in VO₂ kinetics was observed only for creatine kinase (CK) mediated phosphocreatine (PCr) breakdown. Following CK inhibition, faster muscle VO₂ kinetics was observed Thus, in skeletal muscle CK-catalyzed PCr breakdown at contractions onset slows the increase of oxidative phosphorylation. By acting as a high-capacitance energy buffer, PCr breakdown delays or attenuates the increased concentrations of metabolites (such as ADP, Pi, Cr) mediating the VO₂ increase. Upon sudden increases in ATP turnover, skeletal muscle fibers rely first on the bioenergetic pathway (PCr breakdown), which is fast to adjust to increased metabolic needs. Metabolites related to PCr breakdown regulate, but inevitably slow down, the adjustment of oxidative phosphorylation.

Category: iodides-buliding-blocks, 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

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. Application of C2H4INO.

Ghate, Tejashree;Soneji, Kanchan;Barvkar, Vitthal;Ramakrishnan, Padma;Prusty, Debasish;Islam, Sk Ramiz;Manna, Soumen Kanti;Srivastava, Ashish Kumar research published 《 Thiourea mediated ROS-metabolites reprogramming restores root system architecture under arsenic stress in rice》, the research content is summarized as follows. Arsenic (As) is a ubiquitous carcinogenic metalloid that enters into human food chain, through rice consumption. To unravel the conundrum of oxidative vs. reductive stress, the differential root-system architecture (RSA) was studied under As (a ROS producer) and thiourea (TU; a ROS scavenger) alone treatments, which indicated 0.80- and 0.74-fold reduction in the number of lateral roots (NLR), resp. compared with those of control. In case of As+TU treatment, NLR was increased by 4.35-fold compared with those of As-stress, which coincided with partial restoration of redox-status and auxin transport towards the root-tip. The expression levels of 16 ROS related genes, including RBOHC, UPB-1 C, SHR1, PUCHI, were quantified which provided the mol. fingerprint, in accordance with endogenous ROS signature. LC-MS based untargeted and targeted metabolomics data revealed that As-induced oxidative stress was metabolically more challenging than TU alone-induced reductive stress. Cis/trans-ferruloyl putrescine and γ-glutamyl leucine were identified as novel As-responsive metabolites whose levels were decreased and increased, resp. under As+TU than As-treated roots. In addition, the overall amino acid accumulation was increased in As+TU than As-treated roots, indicating the improved nutritional availability. Thus, the study revealed dynamic interplay between ′ROS-metabolites-RSA′, to the broader context of TU-mediated amelioration of As-stress in rice.

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., Application of C2H4INO

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

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. Quality Control of 144-48-9.

Gaun, Aleksandr;Lewis Hardell, Kaitlyn N.;Olsson, Niclas;O’Brien, Jonathon J.;Gollapudi, Sudha;Smith, Megan;McAlister, Graeme;Huguet, Romain;Keyser, Robert;Buffenstein, Rochelle;McAllister, Fiona E. research published 《 Automated 16-Plex Plasma Proteomics with Real-Time Search and Ion Mobility Mass Spectrometry Enables Large-Scale Profiling in Naked Mole-Rats and Mice》, the research content is summarized as follows. Performing large-scale plasma proteome profiling is challenging due to limitations imposed by lengthy preparation and instrument time. We present a fully automated multiplexed proteome profiling platform (AutoMP3) using the Hamilton Vantage liquid handling robot capable of preparing hundreds to thousands of samples. To maximize protein depth in single-shot runs, we combined 16-plex Tandem Mass Tags (TMTpro) with high-field asym. waveform ion mobility spectrometry (FAIMS Pro) and real-time search (RTS). We quantified over 40 proteins/min/sample, doubling the previously published rates. We applied AutoMP3 to investigate the naked mole-rat plasma proteome both as a function of the circadian cycle and in response to UV treatment. In keeping with the lack of synchronized circadian rhythms in naked mole-rats, we find few circadian patterns in plasma proteins over the course of 48 h. Furthermore, we quantify many disparate changes between mice and naked mole-rats at both 48 h and one week after UV exposure. These species differences in plasma protein temporal responses could contribute to the pronounced cancer resistance observed in naked mole-rats. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE [1] partner repository with the dataset identifier PXD022891.

Quality Control 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

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. Related Products of 144-48-9.

Dopp, Jared L.;Reuel, Nigel F. research published 《 Simple, functional, inexpensive cell extract for in vitro prototyping of proteins with disulfide bonds》, the research content is summarized as follows. In vitro expression of proteins from E. coli extract is a useful method for prototyping and production of cytotoxic or unnatural products. However, proteins that have multiple disulfide bonds require custom extract that, to date, requires careful addition of exogenous isomerase enzymes or the use of expensive com. kits. This cost and complexity currently limit access to some groups who wish to rapidly prototype proteins with disulfide bonds. Herein, we present a simple solution that does not require addition of supplemental enzymes. We use a com. available SHuffle T7 Express lysY strain of E. coli that expresses both T7 RNAP and DsbC isomerase enzymes. We exptl. determine optimal growth conditions (IPTG induction and harvest times) to balance overall productivity and efficiency of disulfide bond formation using a luciferase (from Gaussia princeps) that contains five disulfide bonds as our reporter protein. We also demonstrate the ability for rapid prototyping by screening the activity of four putative luciferases against ten luciferin analogs. To display the broad applicability of the extract, three other enzymes containing ≥3 disulfide bonds (hevamine, endochitinase A, and periplasmic AppA) were also expressed from minimal genetic templates that had undergone rolling circle amplification and confirmed via activity assays.

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., Related Products of 144-48-9

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