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Chloroacetamide

Chloroacetamide is a chemical compound with the molecular formula CH3CONHCH2Cl.
It is a halogenated acetamide derivative used in various industrial and agricultural applications, including as a fungicide, herbicide, and intermediate in organic synthesis.
Chloroacetamide has been studied for its potential biological activities and pharmacological properties, with research ongoing to explore its diverse applications.
This compound may be of interest to researchers in fields such as chemistry, toxicology, and environmental science.

Most cited protocols related to «Chloroacetamide»

1
Automated GFP-tagged Protein Purification
Cited 33 times
Cell pellets were thawed on ice and incubated for 30 min at room temperature in 1 ml lysis buffer containing 150 mM NaCl, 50 mM Tris, pH 7.5, 5% glycerol, 1% IGEPAL-CA-630, 1 mM MgCl2, 200 U benzonase (Merck), and EDTA-free complete protease inhibitor cocktail (Roche). When studying phospho-dependent interactions, phosphatase inhibitors (Roche) were added as well. Lysates were cleared by centrifugation at 4,000 g and 4°C for 15 min to remove remaining membrane and DNA, and the supernatant was incubated with 50 µl magnetic beads coupled to monoclonal mouse anti-GFP antibody (Miltenyi Biotec) for 15 min on ice. Because of the extremely small size of the beads (50 nm), they are nonsedimenting and show fast reaction kinetics. Magnetic columns were equilibrated using 250 µl lysis buffer. Cell lysates were added to the column after incubation and washed three times with 800 µl ice-cold wash buffer I containing 150 mM NaCl, 50 mM Tris, pH 7.5, 5% glycerol, and 0.05% IGEPAL-CA-630, and two times with 500 µl of wash buffer II containing 150 mM NaCl, 50 mM Tris, pH 7.5, and 5% glycerol. Purified proteins were predigested by adding 25 µl 2 M urea in 50 mM Tris, pH 7.5, 1 mM DTT, and 150 ng EndoLysC (Wako Chemicals USA, Inc.) for SILAC experiments or 150 ng trypsin (Promega) for label-free experiments. After in-column digestion for 30 min at room temperature, proteins were eluted by adding two times 50 µl 2 M urea in 50 mM Tris, pH 7.5, and 5 mM chloroacetamide. In SILAC experiments, heavy and light eluates of transgenic cell line and the corresponding WT cell line were combined immediately after elution from the columns. Proteins were digested overnight at room temperature. The digestion was stopped by adding 1 µl trifluoroacetic acid, and peptides of each experiment were split and purified on two C18 Stage Tips and stored at 4°C (Rappsilber et al., 2007 (link)).
Pull-downs can be performed manually on a hand magnet. In our laboratory, pull-downs were performed on the automated liquid-handling platform (Freedom EVO 200; Tecan) in a fully automated manner.
Hubner N.C., Bird A.W., Cox J., Splettstoesser B., Bandilla P., Poser I., Hyman A, & Mann M. (2010). Quantitative proteomics combined with BAC TransgeneOmics reveals in vivo protein interactions. The Journal of Cell Biology, 189(4), 739-754.
Publication 2010
Animals, Transgenic Antibodies, Anti-Idiotypic Benzonase Buffers Cell Lines Cells Centrifugation chloroacetamide Cold Temperature Digestion Edetic Acid Glycerin Igepal CA-630 inhibitors Kinetics Lanugo Magnesium Chloride Mice, Laboratory Pellets, Drug Peptides Phosphoric Monoester Hydrolases Promega Protease Inhibitors Proteins Sodium Chloride Tissue, Membrane TNFSF14 protein, human Trifluoroacetic Acid Tromethamine Trypsin Urea
2
Proteomic Workflow for HeLa and E. coli
Cited 14 times
Human cervical cancer cells (HeLa S3, ATCC, Manassas, VA) were grown in Dulbecco's modified Eagle's medium with 10% fetal bovine serum, 20 mm glutamine and 1% penicillin-streptomycin (all Life Technologies Ltd., Paisley, UK). Escherichia coli (strain: XL1 blue) was cultured at 37 °C in LB medium until logarithmic phase (optical density = 0.5, λ = 600 nm). Cells were collected by centrifugation. Following a washing step with cold phosphate buffered saline, they were pelleted and flash frozen in liquid nitrogen and stored at −80 °C.
One-device cell lysis, reduction, and alkylation was performed in sodium deoxycholate (SDC) buffer with chloroacetamide (PreOmics GmbH, Martinsried, Germany) according to our previously published protocol (32 (link)). Briefly, the cell suspension was twice boiled for 10 min at 95 °C and subsequently sonicated for 15 min at maximum energy (Bioruptor, Diagenode, Seraing, Belgium). Proteins were enzymatically hydrolyzed overnight at 37 °C by LysC and trypsin (1:100 enzyme:protein (wt/wt) for both). To stop the digestion, the reaction mixture was acidified with five volumes of isopropanol with 1% trifluoroacetic acid (TFA). Peptides were de-salted and purified in two steps, first on styrenedivinylbenzene-reversed phase sulfonate (SDB-RPS), and second on C18 sorbent. The dried eluates were re-constituted in water with 2% acetonitrile (ACN) and 0.1% TFA for direct LC-MS analysis or high pH reversed-phase fractionation.
For the experiments with the Evosep One (see below), HeLa cell pellets were re-suspended and lysed in water/trifluoroethanol. Disulfide bonds were reduced with dithiothreitol and alkylated with iodoacetamide in ammonium bicarbonate buffer. Following tryptic digestion, the peptide mixture was de-salted and purified on C18 sorbent.
Meier F., Brunner A.D., Koch S., Koch H., Lubeck M., Krause M., Goedecke N., Decker J., Kosinski T., Park M.A., Bache N., Hoerning O., Cox J., Räther O, & Mann M. (2018). Online Parallel Accumulation–Serial Fragmentation (PASEF) with a Novel Trapped Ion Mobility Mass Spectrometer. Molecular & Cellular Proteomics : MCP, 17(12), 2534-2545.
Publication 2018
acetonitrile Alkanesulfonates Alkylation ammonium bicarbonate Buffers Cells Centrifugation Cervical Cancer chloroacetamide Cold Temperature Culture Media Deoxycholic Acid, Monosodium Salt Digestion Disulfides Dithiothreitol Enzymes Escherichia coli Fetal Bovine Serum Fractionation, Chemical Freezing Glutamine HeLa Cells Homo sapiens Iodoacetamide Isopropyl Alcohol Medical Devices Nitrogen Pellets, Drug Penicillins Peptides Phosphates Proteins Saline Solution Strains Streptomycin Trifluoroacetic Acid Trifluoroethanol Trypsin
3
Plasma Proteome Sample Preparation
Cited 10 times
Plasma sample preparation was performed
according the protocol
in the Supporting Methods, which was adapted
from 3 previous studies.17 (link)−19 (link) All steps in this protocol were
completed without the aid of any robotics. Briefly, 1 μL of
plasma (60–70 μg protein) was added to 24 μL of
SDC buffer (1% sodium deoxycholate, 10 mM TCEP, 40 mM chloroacetamide,
and 100 mM Tris-HCl pH 8.5) in either a 500 μL 96-well
Protein Lo-bind plate, or Protein Lo-bind 1.5 mL tubes (Eppendorf).
After sealing the tube or plate (with a silicone mat, Eppendorf),
samples were heated to 95 °C for 10 min at 1,000 rpm in an Eppendorf
Thermomixer-C with a ThermoTop (heated lid) to denature, reduce, and
alkylate proteins. Once cooled to RT and diluted 10-fold with water,
LysC and Trypsin were added (from 1 mg/mL stock solutions in either
water, or 50 mM acetic acid, respectively) to digest proteins at 1:100
ratio (each protease:protein, μg/μg) and digested at 37
°C for 16 h at 1000 rpm in an Eppendorf Thermomixer-C with a
ThermoTop (heated lid). An equal volume (250 μL) of 99% ethyl
acetate/1% TFA was added to the digested peptides for a final concentration
of 49.5% ethyl acetate and 0.5% TFA.
SDB-RPS StageTips were
generated by punching double-stacked SDB-RPS discs (Sigma, Cat # 66886-U)
with an 18-gauge needle and mounted in 200 μL tips (Eppendorf),
as shown in Supporting Methods. For StageTip
SPE processing using the Spin96, StageTips were inserted into a holder
and placed in the top, which was then stacked onto the wash-bottom
containing a polypropylene 96-well microtiter plate to collect the
sample flow-through and washes (Figure S1a). Each tip was wetted with 100 μL of 100% acetonitrile and
centrifuged at 1000g for 1 min. Following wetting,
each StageTip was equilibrated with 100 μL of 0.1% TFA in H2O
and 30% methanol/1% TFA with centrifugation for each at 1000g for 3 min. Each StageTip was then loaded with the equivalent
of ∼10 μg peptide in 49.5% ethyl acetate and 0.5% TFA
(equal volumes of each phase used). The peptides were washed twice
with 100 μL of 99% ethyl acetate/1% TFA, which was followed
by one wash with 100 μL of 0.2% TFA in water. For elution of
peptides, the wash-bottom was exchanged with a bottom containing a
holder supporting an unskirted PCR plate that has been trimmed to
fit (Figure S1b). To elute, 100 μL
of 5% ammonium hydroxide/80% acetonitrile was added to each tip and
centrifuged as above for 5 min. Samples in the PCR plate were dried
using a GeneVac EZ-2 using the ammonia setting at 40 °C for 1
h. Dried peptides were resuspended in 30 μL of 5% formic acid
and a CBQCA assay (see below) was performed to ensure even sample
loading. Samples were then stored at 4 °C until analyzed by LC–MS.
Harney D.J., Hutchison A.T., Hatchwell L., Humphrey S.J., James D.E., Hocking S., Heilbronn L.K, & Larance M. (2019). Proteomic Analysis of Human Plasma during Intermittent Fasting. Journal of Proteome Research, 18(5), 2228-2240.
Publication 2019
3-(4-carboxybenzoyl)-2-quinolinecarboxaldehyde Acetic Acid acetonitrile Ammonia Ammonium Hydroxide Biological Assay Buffers Centrifugation chloroacetamide Deoxycholic Acid, Monosodium Salt ethyl acetate Methanol Needles Peptide Hydrolases Peptides Plasma Polypropylenes Proteins Silicones tris(2-carboxyethyl)phosphine Tromethamine Trypsin
4
Bead-Based Protein Digestion Protocol
Cited 8 times
Proteins were aggregated on microspheres and washed as described above. For on-bead digestion, 50 mm HEPES buffer (pH 8.5) was added to submerge microspheres. Proteins were reduced and alkylated with the 5 mm tris(2-carboxyethyl)phosphine (TCEP) and 5.5 mm 2-chloroacetamide (CAA) for 30 min if not treated immediately after lysis. Lys-c (Wako Chemicals) was added at ratio of 1:200 (to protein) and allowed to react for 1 h at 37 °C followed by the addition of trypsin at a ratio of 1:100 (unless specified otherwise). Trypsin digestion was allowed to occur overnight at 37 °C. Beads were separated by magnet and the supernatant was transferred to new tube and acidified.
In-solution digestion with guanidine hydrochloride buffer was carried out under similar reduction and alkylation conditions. Lys-c was added to solution and allowed to react for 1 h at 37 °C. The concentration of guanidine hydrochloride concentration was reduced to >1 M before the addition of trypsin for overnight digestion. Solution was acidified by with 1% trifluoroacetic acid (TFA) and centrifuged for 5 min at 5000 × g and the supernatant transferred to new tubes.
Peptide mixtures were clarified with solid phase extraction. Briefly, hydrophobic C18 sep-pak (Waters Corporation, Taastrup, Denmark) were prepared by washing with acetonitrile and 0.1% TFA, followed by loading of the acidified peptide mixtures by gravity. Sep-paks were washed with 0.1% TFA and peptides were eluted using 50% Acetonitrile (0.05% TFA). Organic solvent was evaporated and peptides concentrated using a speedvac before MS analysis.
Batth T.S., Tollenaere M.A., Rüther P., Gonzalez-Franquesa A., Prabhakar B.S., Bekker-Jensen S., Deshmukh A.S, & Olsen J.V. (2019). Protein Aggregation Capture on Microparticles Enables Multipurpose Proteomics Sample Preparation. Molecular & Cellular Proteomics : MCP, 18(5), 1027-1035.
Publication 2019
acetonitrile Alkylation Buffers chloroacetamide Digestion Gravity HEPES Hydrochloride, Guanidine Microspheres Peptides phosphine Proteins PRSS1 protein, human Solid Phase Extraction Solvents Trifluoroacetic Acid tris(2-carboxyethyl)phosphine Tromethamine Trypsin
5
Comprehensive Proteomic Sample Preparation
Cited 7 times
From 20 to 25 µg of proteins (based on two lowest temperatures in case TPP experiments, and NP40-processed vehicle-treated samples in case of SPP experiments) from the supernatant were reduced, alkylated, and digested with Trypsin and LysC using modified SP3 protocol50 (link). Briefly, proteins samples were bound to acidified paramagnetic beads (0.5 µg Sera-Mag-beads A and B in 10 µl of 15% formic acid and 30 µl ethanol). Following an incubation of 15 min, the protein-bound beads were washed four times with 70% ethanol. On bead reduction, alkylation, and digestion of the proteins were performed overnight using 0.25 µg Trypsin, 0.25 µg LysC, 1.7 mM TCEP, and 5 mM chloroacetamide in 100 mM HEPES, pH 8. Subsequently, the peptides were eluted from the beads and lyophilized. The dried peptides were dissolved with 10 µl water and 10 µl of TMT labels (8 µg per µl) was added and incubated for 60 min. The labelling reactions were quenched with 5 µl hydroxylamine (2.5%) solution and pooled together and vacuum dried for LC-MS-MS analysis.
For TPP-temperature range experiments, sample from 10 different temperatures were labelled with 10 different TMT tags and pooled together as a single TMT experiment. In a 2D-TPP experiment, the concentration range of two neighboring temperatures were labelled and pooled as a single TMT experiment. In case of SPP experiment, nine NP40-processed (one vehicle and eight small molecule treated) samples and one SDS-processed (vehicle) sample were labelled and pooled as a single TMT experiment.
Dried peptide samples were reconstituted in 1.25% ammonia in water and fractionated on an Ultimate3000 (Dionex) by reversed-phase chromatography at pH 12 (Buffer A: 20 mM Ammonium formate pH 10, Buffer B: Acetonitrile) on X-bridge column (2.1 × 10 mm, C18, 3.5 µm, Waters, Milford, MA), and 24 fractions were collected and vacuum dried.
Sridharan S., Kurzawa N., Werner T., Günthner I., Helm D., Huber W., Bantscheff M, & Savitski M.M. (2019). Proteome-wide solubility and thermal stability profiling reveals distinct regulatory roles for ATP. Nature Communications, 10, 1155.
Publication 2019
acetonitrile Alkylation Ammonia Buffers chloroacetamide Chromatography, Reverse-Phase Cold Temperature Ethanol formic acid formic acid, ammonium salt HEPES Hydroxylamine Peptides Protein Digestion Proteins Serum Tandem Mass Spectrometry tris(2-carboxyethyl)phosphine Trypsin Vacuum

Most recents protocols related to «Chloroacetamide»

1
Synthesis of Substituted Acetamides
A mixture of 1 (3.95 g, 10 mmol), methyl iodide (0.7 mL, 10 mmol), ethyl chloroacetate (1 mL, 10 mmol), 2-chloroacetamide (0.93 g, 10 mmol), chloroacetonitrile (0.8 mL, 10 mmol)or N-aryl-2-chloroacetamide 2a–e (10 mmol), and sodium acetate trihydrate (1.50 g, 11 mmol) in ethanol (100 mL) was refluxed for one hour. The reaction mixture was then allowed to stand at room temperature overnight. After that the precipitate was collected and recrystallized from ethanol as colorless crystals of title compounds 3, 4, 5, 6, and 7a–e respectively.
Sayed E.M., Bakhite E.A., Hassanien R., Farhan N., Aly H.F., Morsy S.G, & Hassan N.A. (2024). Novel tetrahydroisoquinolines as DHFR and CDK2 inhibitors: synthesis, characterization, anticancer activity and antioxidant properties. BMC Chemistry, 18(1), 34.
Publication 2024
2
Synthesis of Phenylacetamide Derivatives
To a solution of 1 mmol aniline/benzylamine derivatives in 4 ml DMF, 1 mmol chloroacetylchloride was added at 0 °C. The mixture was stirred at room temperature for 5 h and poured into water and then filtered to get phenylacetamide derivatives. The obtained solids were then filtered, dried, and recrystallized from ethanol.
Khaleghi N., Esmkhani M., Noori M., Dastyafteh N., Ghomi M.K., Mahdavi M., Sayahi M.H, & Javanshir S. (2024). Copper supported modified magnetic carrageenan as a bio-based catalyst for the synthesis of novel scaffolds bearing the 1,2,3-triazole unit through the click reaction. Nanoscale Advances, 6(9), 2337-2349.
Publication 2024
3
Protein Denaturation and Tryptic Digestion
For analysis by MS, 100 µl denaturation solution (4 M urea, 100 mM Tris–HCl (pH 7.5), 2 mM DTT and 10 mM chloroacetamide) were added per 100 mg plug in a 1.5 ml tube. After vortexing, samples were incubated at 37 °C for 30 min with agitation (1,500 rpm). Then, 20 µl trypsin solution (2 M urea, 50 mM Tris–HCl (pH 7.5), 1 mM DTT, 5 mM chloroacetamide and 20 µg ml−1 trypsin (Sigma-Aldrich)) was added per sample. After overnight incubation at 25 °C with rapid agitation (1,500 rpm), samples were centrifuged at high speed for 10 min. Supernatants were transferred to fresh tubes. Trifluoroacetic acid (TFA) was added at 1% (final concentration).
Carnie C.J., Acampora A.C., Bader A.S., Erdenebat C., Zhao S., Bitensky E., van den Heuvel D., Parnas A., Gupta V., D’Alessandro G., Sczaniecka-Clift M., Weickert P., Aygenli F., Götz M.J., Cordes J., Esain-Garcia I., Melidis L., Wondergem A.P., Lam S., Robles M.S., Balasubramanian S., Adar S., Luijsterburg M.S., Jackson S.P, & Stingele J. (2024). Transcription-coupled repair of DNA–protein cross-links depends on CSA and CSB. Nature Cell Biology, 26(5), 797-810.
Publication 2024
4
Synthesis of N-Aryl Pyrazoles
A mixture of 1 (3.95 g, 10 mmol), N-aryl-2-chloroacetamide 2a–e (10 mmol) and anhydrous sodium carbonate (1.35 g) in ethanol (100 mL) was refluxed for three hours. The precipitate that formed on cooling was collected and recrystallized from dioxane as yellow crystals of 8a–e (94–98%).
Sayed E.M., Bakhite E.A., Hassanien R., Farhan N., Aly H.F., Morsy S.G, & Hassan N.A. (2024). Novel tetrahydroisoquinolines as DHFR and CDK2 inhibitors: synthesis, characterization, anticancer activity and antioxidant properties. BMC Chemistry, 18(1), 34.
Publication 2024
5
Proteomic Characterization of Recombinant EtpA
Recombinant EtpA glycoprotein was exchanged to water using Microcon Ultracel PL-10 centrifugal filter. Glycoprotein was reduced with 5 mM tris(2-carboxyethyl) phosphine hydrochloride (TCEP-HCl) and alkylated with 10 mM 2-Chloroacetamide in 100 mM ammonium acetate for 20 min at room temperature (RT, 24°C). Glycoprotein was digested with 1:25 Proteinase K (PK) for 30 min at 37°C or 1:20 trypsin for 16 h at 37°C. Proteases (PK/trypsin) were denatured by incubating at 90°C for 15 min, further diluted in buffer A, subsequently analyzed by LC-MS/MS.
Proteinase K and trypsin treatment: recombinant EtpA glycoprotein was exchanged to water using Microcon Ultracel PL-10 centrifugal filter. Glycoprotein was reduced with 5 mM tris(2-carboxyethyl) phosphine hydrochloride (TCEP-HCl) and alkylated with 10 mM 2-Chloroacetamide in 100 mM ammonium acetate for 20 min at room temperature (RT, 24°C). Glycoprotein was digested with 1:25 Proteinase K (PK) for 30 min at 37°C or 1:20 trypsin for 16 h at 37°C. Proteases (PK/trypsin) were denatured by incubating at 90°C for 15 min, further diluted in buffer A, subsequently analyzed by LC-MS/MS
Berndsen Z.T., Akhtar M., Thapa M., Vickers T., Schmitz A., Torres J.L., Baboo S., Kumar P., Khatoom N., Sheikh A., Hamrick M., Diedrich J.K., Martinez-Bartolome S., Garrett P.T., Yates JR I.I.I., Turner J.S., Laird R.M., Poly F., Porter C.K., Copps J., Ellebedy A.H., Ward A.B, & Fleckenstein J.M. (2024). Repeat modules and N-linked glycans define structure and antigenicity of a critical enterotoxigenic E. coli adhesin. bioRxiv.
Publication Preprint 2024

Top products related to «Chloroacetamide»

1
Trypsin by Promega
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Trypsin is a serine protease enzyme that is commonly used in cell culture and molecular biology applications. It functions by cleaving peptide bonds at the carboxyl side of arginine and lysine residues, which facilitates the dissociation of adherent cells from cell culture surfaces and the digestion of proteins.
2
Lys c by Fujifilm
Sourced in Japan, United States, Germany
Lys-C is a protease enzyme used in proteomics research. It selectively cleaves proteins at the carboxyl side of lysine residues, which can be useful for generating peptide fragments for analysis.
3
Sequencing grade modified trypsin by Promega
Sourced in United States, United Kingdom, Germany, France, Switzerland, Japan, China, Sweden
Sequencing grade modified trypsin is a protease enzyme used for the digestion of proteins prior to mass spectrometry analysis. It is designed to provide consistent, high-quality peptide digestion for protein identification and characterization.
4
Chloroacetamide by Merck Group
Sourced in United States, Germany
Chloroacetamide is a chemical compound used in laboratory settings. It functions as a reagent or intermediate in various organic synthesis reactions. The core property of Chloroacetamide is its ability to participate in chemical transformations, making it a useful tool for researchers and chemists.
5
2 chloroacetamide by Merck Group
Sourced in United States
2-chloroacetamide is a chemical compound used as a laboratory reagent. It is a white crystalline solid with the molecular formula C2H4ClNO. The core function of 2-chloroacetamide is to serve as a chemical intermediate and building block in various organic synthesis reactions.
6
Trypsin by Merck Group
Sourced in United States, Germany, United Kingdom, China, Italy, Japan, Sao Tome and Principe, Canada, Macao, Poland, India, France, Spain, Portugal, Australia, Switzerland, Ireland, Belgium, Sweden, Israel, Brazil, Czechia, Denmark, Austria
Trypsin is a serine protease enzyme that is commonly used in cell biology and biochemistry laboratories. Its primary function is to facilitate the dissociation and disaggregation of adherent cells, allowing for the passive release of cells from a surface or substrate. Trypsin is widely utilized in various cell culture applications, such as subculturing and passaging of adherent cell lines.
7
Sequencing grade trypsin by Promega
Sourced in United States, Germany, United Kingdom, Italy, France, Spain, Switzerland
Sequencing grade trypsin is a proteolytic enzyme used to cleave peptide bonds in protein samples, primarily for use in protein sequencing applications. It is purified to ensure high-quality, consistent performance for analytical processes.
8
Sep pak c18 cartridge by Waters Corporation
Sourced in United States, Italy, Ireland, United Kingdom, Canada, Germany
The Sep-Pak C18 cartridge is a solid-phase extraction (SPE) device used for sample preparation in analytical chemistry. It is designed to selectively retain and concentrate analytes of interest from complex matrices prior to instrumental analysis.
9
Trypsin gold by Promega
Sourced in United States, United Kingdom, Germany, Switzerland, Australia, Spain
Trypsin Gold is a highly purified serine protease enzyme commonly used for the dissociation and detachment of adherent cells in cell culture applications. It effectively cleaves peptide bonds at the carboxyl side of lysine and arginine residues.
10
Trypsin lys c by Promega
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Trypsin/Lys-C is a dual-specificity protease that cleaves peptide bonds primarily at the carboxyl side of lysine and arginine residues. It is commonly used in protein sample preparation for mass spectrometry analysis.

More about "Chloroacetamide"

Chloroacetamide is a versatile chemical compound with the molecular formula CH3CONHCH2Cl.
It is a halogenated acetamide derivative that finds various industrial and agricultural applications, including use as a fungicide, herbicide, and intermediate in organic synthesis.
Researchers have studied Chloroacetamide's potential biological activities and pharmacological properties, exploring its diverse uses in fields like chemistry, toxicology, and environmental science.
Related compounds and terms include 2-chloroacetamide, which is a structural isomer, and Sequencing grade trypsin, a protease enzyme often used in conjunction with Chloroacetamide for protein sample preparation and analysis.
Trypsin, Lys-C, and Sequencing grade modified trypsin are other proteases that may be utilized in similar workflows.
Sep-Pak C18 cartridges are a common tool for sample clean-up and purification when working with Chloroacetamide and related compounds.
Optimizing Chloroacetamide research can be facilitated by AI-driven protocol comparisons and analysis tools, such as those offered by PubCompare.ai.
This innovative platform helps researchers identify the best procedures from literature, preprints, and patents, improving experimental reproducibility and streamlining the research process.
With the insights gained, scientists can navigate the diverse applications and studies surrounding Chloroacetamide more effectively.