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Water

Water is an essential component of life, covering approximately 71% of the Earth's surface.
It serves as a vital medium for numerous biological processes, facilitating the transport of nutrients, regulating temperature, and enabling chemical reactions.
In the field of water research, scientists and researchers explore the properties, distribution, and interactions of this fundamental resource.
PubCompare.ai streamlines this workflow by providing a user-frindly platform to easily locate the best protocols from literature, pre-prints, and patents, while leveraging AI-driven comparisons to optimize reproducibility and identify the ideal products for water-related experiments.
This powerful tool empowers researchers to take their water research to new heights, unlocking new discoveries and advancements in this critical domain.

Most cited protocols related to «Water»

DNase treatment, cDNA synthesis, primer design and SYBR Green I RT-PCR were carried out as described [23 (link)]. In brief, 2 μg of each total RNA sample was treated with the RQ1 RNase-free DNase according to the manufacturer's instructions (Promega). Treated RNA samples were desalted (to prevent carry over of magnesium) before cDNA synthesis using Microcon-100 spin columns (Millipore). First-strand cDNA was synthesized using random hexamers and SuperscriptII reverse transcriptase according to the manufacturer's instructions (Invitrogen), and subsequently diluted with nuclease-free water (Sigma) to 12.5 ng/μl cDNA. RT-PCR amplification mixtures (25 μl) contained 25 ng template cDNA, 2x SYBR Green I Master Mix buffer (12.5 μl) (Applied Biosystems) and 300 nM forward and reverse primer. Reactions were run on an ABI PRISM 5700 Sequence Detector (Applied Biosystems). The cycling conditions comprised 10 min polymerase activation at 95°C and 40 cycles at 95°C for 15 sec and 60°C for 60 sec. Each assay included (in duplicate): a standard curve of four serial dilution points of SK-N-SH or IMR-32 cDNA (ranging from 50 ng to 50 pg), a no-template control, and 25 ng of each test cDNA. All PCR efficiencies were above 95%. Sequence Detection Software (version 1.3) (Applied Biosystems) results were exported as tab-delimited text files and imported into Microsoft Excel for further analysis. The median coefficient of variation (based on calculated quantities) of duplicated samples was 6%.
Publication 2002
Anabolism Biological Assay Buffers Deoxyribonucleases DNA, Complementary Endoribonucleases Magnesium Oligonucleotide Primers prisma Promega Reverse Transcriptase Polymerase Chain Reaction RNA-Directed DNA Polymerase SYBR Green I Technique, Dilution
Class I additive force fields (see equation 1), which do not explicitly treat electronic polarization, have been designed for use in polar environments typically found in proteins and in solution. To achieve this, the use of experimental target data, supplemented by QM data, was strongly emphasized during optimization of the nonbonded parameters in the biomolecular CHARMM force fields, in order to ensure physical behavior in the bulk phase. However, reproducing experimental data requires molecular dynamics (MD) simulations, which have to be set up carefully and repeated multiple times in the course of the parametrization, making the usage of experimental target data non-trivial and time-consuming. In addition, for many functional groups that may occur in drug-like molecules experimental data may not be available. Due to this lack of data, and since one of the main goals of CGenFF is easy and fast extensibility, a slightly different philosophy was adapted, with more emphasis on QM results as target data for parameter optimization. This is possible due to the wide range of functionalities already available whose parameters were optimized based largely on experimental data, along with the establishment of empirical scaling factors that can be applied to QM data in order to make them relevant for the bulk phase.
The only cases where experimental data would be required are situations where novel atom types are present for which LJ parameters are not already available in CGenFF. These cases would require optimization of the LJ parameters, supplemented with Hartree-Fock (HF) model compound-water minimum interaction energies and distances (see step 2.a under “Generation of target data for parameter validation and optimization” and step 1 under “Parametrization procedure”), based on the reproduction of bulk phase properties, typically pure solvent molecular volumes and heats of vaporization or crystal lattice parameters and heats of sublimation. Descriptions of the optimization protocol have been published previously.7 ,9 ,25 (link) However, it should be noted that CGenFF has been designed to cover the majority of atom types in pharmaceutical compounds, such that optimization of LJ parameters is typically not required.
The remainder of this section includes 1) the procedure to add new model compounds and chemical groups to the force field, 2) the procedure for generating the QM target data, and 3) the procedure for application of the QM information to parametrize new molecules. To put these procedures in better context, example systems including pyrollidine, the addition of substituents to pyrollidine and the development of a linker between pyrollidine and benzene are presented.
Publication 2010
Benzene Dietary Fiber Pharmaceutical Preparations Physical Examination Proteins Reproduction Solvents Vaporization
The C36m FF was validated using a variety of systems including peptides, IDPs, unfolded states of proteins, and globular proteins. The CHARMM-modified TIP3P model35 was used in all simulations, unless noted. All the systems studied here are in high dilution such that the systems did not test the force fields with respect to aggregation. A summary of the validation simulations is given in the Supplementary Table 1, and detailed information of setup and analysis for each simulation system is given in the Supplementary Note. Briefly, temperature replica exchange (T-REX) simulations were carried out with GROMACS36 for the RS peptide (0.63 μs * 34 replica), the GB1 hairpin (0.8 μs * 32 replica), the Nrf2 hairpin (1 μs * 28 replica), Chignolin (6 μs * 29 replica) and CLN025 (6 μs * 29 replica). Hamiltonian replica exchange (HREX) simulation was carried out with CHARMM37 for polyQ using the end-to-end distance as the biasing reaction coordinate. Harmonic umbrella potentials with a force constant of 0.2 kcal/mol/Å2 were applied to target end-to-end distances ranging from 5 to 75 Å spaced at 5 Å intervals. Similar H-REX protocol using distance as the biasing reaction coordinate was applied to study the folding free energy of HP21. Conformations were also sampled using single, long MD trajectories with OpenMM,38 including 5 μs simulations for the HEWL19 peptide, IN and CspTm, 10 μs simulations for the (AGQ)n peptides, and 16 μs simulations for (AAQAA)3. A 1.2 μs simulation of ubiquitin was carried out with NAMD to compare with previous results using the C36 FF.39 Alternative water models were tested with the RS peptide using T-REX simulations (0.63 μs * 34 replica) and with IN and CspTm using 5 μs MD simulations.
Analysis of MD trajectories was carried out using GROMACS36 or CHARMM.37 A left-handed α-helix is defined as having at least three consecutive residues with φ, ψ~falling in the αL region (30°<φ<100° and 7°<ψ< 67°, Supplementary Fig. 20). The αL probability is computed as the fraction of the ensemble containing left α-helix as in Ref.32 We also compute the αL fraction as the probability for residues to be in a left-handed α-helix, and the αL propensity as the probability for residues’ φ, ψ to be in the αL region, as additional measurement of α-left helix sampling.
Publication 2016
chignolin Eye Helix (Snails) IDH2, human NFE2L2 protein, human Peptides polyglutamine Proteins Technique, Dilution Ubiquitin YYDPETGTWY
MD simulations of hen egg white lysozyme (HEWL), bovine pancreatic trypsin inhibitor (BPTI), ubiquitin (Ubq), and the B3 domain of Protein G (GB3) were performed using Desmond version 2.1.0.1 and the Amber ff99SB or the modified Amber ff99SB-ILDN force fields. The TIP3P water model20 was used for simulations of HEWL, Ubq, and GB3, and the TIP4P-Ew water model21 (link) was used for simulations of BPTI. Simulation parameters were the same as in the simulations of small helical peptides, apart from the fact that a 643 PME grid was used for HEWL and a 483 grid was used for BPTI, Ubq, and GB3. Simulations of HEWL, BPTI, Ubq, and GB3 were initiated from PDB22 (link) entries 6LYT, 5PTI, 1UBQ, and 1P7E solvated in cubic water boxes containing 10,594, 4215, 6080, and 5156 water molecules, respectively. The net charge of the proteins was neutralized with sodium or chloride ions. Each system was initially subject to energy minimization, followed by 1.2 ns of MD simulation in the NPT ensemble during which the temperature was increased linearly from 10 to 300 K, and position restraints on the backbone atoms were annealed from 1.0 to 0.0 kcal mol−1 Å−1. After this initial relaxation, each system was simulated for 6 ns in the NPT ensemble. The frame of this simulation with the volume closest to the average volume was selected as the starting conformation for a production run of 1.2 μs in the NVT ensemble. The trajectories obtained from the NVT runs were used for subsequent data analysis.
Publication 2010
Amber Aprotinin Chlorides Cuboid Bone Helix (Snails) hen egg lysozyme Ions Peptides Protein Domain Proteins Reading Frames Sodium Ubiquitin Vertebral Column
The streptavidin alkaline phosphatase method was adapted to detect the viral antigen using a polyclonal anti-ZIKV antibody produced at the Evandro Chagas Institute2 (link). The biotin-streptavidin peroxidase method was used for immunostaining of tissues with antibodies specific for each marker studied. First, the tissue samples were deparaffinized in xylene and hydrated in a decreasing ethanol series (90%, 80%, and 70%). Endogenous peroxidase was blocked by incubating the sections in 3% hydrogen peroxide for 45 min. Antigen retrieval was performed by incubation in citrate buffer, pH 6.0, or EDTA, pH 9.0, for 20 min at 90 °C. Nonspecific proteins were blocked by incubating the sections in 10% skim milk for 30 min. The histological sections were then incubated overnight with the primary antibodies diluted in 1% bovine serum albumin (Supplementary Table S1). After this period, the slides were immersed in 1 × PBS and incubated with the secondary biotinylated antibody (LSAB, DakoCytomation) in an oven for 30 min at 37 °C. The slides were again immersed in 1X PBS and incubated with streptavidin peroxidase (LSAB, DakoCytomation) for 30 min at 37 °C. The reactions were developed with 0.03% diaminobenzidine and 3% hydrogen peroxide as the chromogen solution. After this step, the slides were washed in distilled water and counterstained with Harris hematoxylin for 1 min. Finally, the sections were dehydrated in an increasing ethanol series and cleared in xylene.
Publication 2018
Alkaline Phosphatase Antibodies Antibodies, Anti-Idiotypic Antigens Antigens, Viral azo rubin S Biotin Buffers Citrates Edetic Acid Ethanol Hematoxylin Immunoglobulins Milk, Cow's Peroxidase Peroxide, Hydrogen Peroxides Proteins Serum Albumin, Bovine Streptavidin Tissues Tritium Xylene Zika Virus

Most recents protocols related to «Water»

Example 30

[Figure (not displayed)]

To a stirred solution of 3-(3,4-dimethoxyphenyl)-5-(4-piperidyl)-1,2,4-oxadiazole (150 mg, 518 μmol) in N,N-dimethylformamide (1.50 mL) were added (2-(1H-benzotriazol-1-yl)-1,1,3,3-tetramethyluronium hexafluorophosphate) (196 mg, 518 μmol), N-ethyl-N-(propan-2-yl)propan-2-amine (201 mg, 1.56 mmol, 271 μL), and 2-(benzylamino)acetic acid (89 mg, 544 μmol). The mixture was stirred at 20° C. for 16 h and filtered, and the crude filtrate was purified directly by prep-HPLC (column: Luna C8 100×30 5 μm; mobile phase: [water (10 mM ammonium carbonate)-acetonitrile]; B%: 30%-60%, 12 min) to give 2-(benzylamino)-1-[4-[3-(3,4-dimethoxyphenyl)-1,2,4-oxadiazol-5-yl]-1-piperidyl]ethanone (48 mg, 110 μmol, 21%) as a yellow solid. 1H NMR (400 MHz, METHANOL-d4) δ=7.65 (dd, J=1.8, 8.2 Hz, 1H), 7.57 (d, J=1.8 Hz, 1H), 7.40-7.30 (m, 4H), 7.28-7.22 (m, 1H), 7.06 (d, J=8.4 Hz, 1H), 4.45 (br d, J=13.7 Hz, 1H), 3.94-3.83 (m, 7H), 3.78 (s, 2H), 3.57-3.44 (m, 2H), 3.40-3.33 (m, 1H), 3.27-3.20 (m, 1H), 3.01 (t, J=11.2 Hz, 1H), 2.17 (dd, J=2.8, 13.3 Hz, 2H), 1.93-1.73 (m, 2H); LCMS (ESI) m/z: [M+H]+=437.3.

Patent 2024
1H NMR Acetic Acid acetonitrile Amines ammonium carbonate Dimethylformamide High-Performance Liquid Chromatographies Lincomycin Methanol Oxadiazoles

Example 1

A 1 g compressed SAM sheet was formed without embossing. To ensure that Comparative Example 1 had the same compactness as Example 1, meaning that both samples experienced the same compressing pressure, the SAM sheets were each placed between two flat metal plates and compressed twice with a 1000 lb load for 10 minutes using the Carver hydraulic compressor (CE, Model 4350). In this way, the void volumes between and within SAM particles are quite close, if not the same, for Comparative Example 1 and Example 1. The sample was dried in a convection oven at 80° C. for 12 hours before testing.

A 1 g compressed SAM sheet was formed without embossing. The prepared SAM sheet was placed on a flat metal plate, covered with a 1″×1″ metal patterned plate with protruding balls of 250 μm diameter, the balls side facing downward towards the SAM sheet (FIG. 1). The Carver hydraulic compressor (CE, Model 4350) was used to create the embossing pattern by applying a 1000 lb load to a plasticized SAM sheet for 5 minutes. After that, the SAM sheet was flipped over and compressed one more time with the metal balls under same pressure and same dwell time. The resultant SAM sheet has a clear pattern on the surface (FIG. 2). The scale bar shows the diameter of dent of 243 μm. The size of the dent is consistent with the size of metal balls of the embossing plate.

The final 1 g compressed SAM sheet had two-sided embossing. The sample was dried in a convection oven at 80° C. for 12 hours before testing.

The protrusions of this example were ball-shaped, but the protrusion of the pins could be any shape. Shapes without sharper corners, such as spheres, could be less damaging to the SAM particles. The depth of the indentations from the shapes could be in the range of from about 10 μm to 200

Absorbency Evaluation.

Equal masses of embossed and non-embossed SAM sheet samples were each individually dropped in a 100 mL beaker containing 30 mL NaCl solution, which contained blue dye to improve visualization during testing. The time and process of the SAM sheet completely absorbing the saline solution was monitored and compared.

The testing process for both samples to compare their absorbency properties is shown in FIGS. 3a-3e. FIG. 3a shows the testing beakers with 30 mL NaCl solution and blue dye. FIG. 3b shows at the start of the testing (0 min) by adding SAM sheets into the respective NaCl solutions. FIG. 3c shows the completion of absorption of liquid for Example 1 at 27 minutes. After completion, the swollen SAM particles were cast off onto white paper to verify the complete absorption of the fluid (FIG. 3d). At 40 min, Comparative Example 1 completed absorbing all fluid and was cast off onto white paper to verify completion (FIG. 3e). By the time Comparative Example 1 was cast off onto white paper, Example 1 had already turned white because it had finished the absorbing process 13 minutes earlier and the absorbed fluid already diffused into the center of each SAM particle. Absorbency times are summarized in Table 1.

TABLE 1
Absorbency times for SAM sheets.
SampleIntake time (min)
Comparative Example 140
Example 127

Compressing SAM particles into sheets generally leads to lower intake rates and higher intake times compared with SAM particles that are not compressed into sheets due to the loss of free volume within SAM molecular structure and surface area. However, the results demonstrated herein prove that SAM with surface embossing could lead to increase of surface area, thereby increasing the absorbency intake rate compared to the compressed SAM without embossing.

Flexible Absorbent Binder Film.

FAB is a proprietary crosslinked acrylic acid copolymer that develops absorbency properties after it is applied to a substrate and dried, FAB itself can also be casted into film and dried, yet the resultant 100% FAB film is quite rigid and stiff. The chemistry of FAB is similar to standard SAPs except that the latent crosslinking component allows it to be applied onto the substrate of choice as an aqueous solution and then converted into a superabsorbent coating upon drying. When the water is removed, the crosslinker molecules in the polymeric chain come into contact with each other and covalently bond to form a crosslinked absorbent.

In the examples of this disclosure, FAB was coated on a nonwoven substrate to provide a single layer with both intake and retention functions, as well as flexibility. FAB solution with 32% (wt/wt) solids was coated on a nonwoven substrate through a slot die with two rolls. After coating, the coated film was cured by drying in a convection oven at 55° C. for 20-30 minutes, or until the film was dry, to remove the water.

Compression embossing was applied on FAB films. Two-sided embossing was applied on a FAB film. The absorbent properties were characterized and compared through saline absorption testing. The FAB film with an embossed pattern showed 91.67% faster intake rate compared with the FAB film without an embossed pattern.

Patent 2024
acrylate Convection Electroplating Metals Molecular Structure Muscle Rigidity Polymers Pressure Retention (Psychology) Saline Solution SKAP2 protein, human Sodium Chloride Urination

Example 1

Provided is a preparation method for an A-site high-entropy nanometer metal oxide (Gd0.4Er0.3La0.4Nd0.5Y0.4)(Zr0.7, Sn0.8, V0.5)O7 with high conductivity, the method including the following steps.

    • (1) Gd(NO3)3, Er(NO3)3, La(NO3)3, Nd(NO3)3, Y(NO3)3, ZrOSO4, SnC14 and NH4VO3 were taken at a molar ratio of 0.4:0.3:0.4:0.5:0.4:0.7:0.8:0.5, added to a mixed solution of deionized water/absolute ethyl alcohol/tetrahydrofuran at a mass ratio of 0.3:3:0.5, and stirred for five minutes to obtain a mixed liquid I. The ratio of the total mass of Gd(NO3)3, Er(NO3)3, La(NO3)3, Nd(NO3)3, Y(NO3)3, ZrOSO4, SnC14 and NH4VO3 to that of the mixed solution of deionized water/absolute ethyl alcohol/tetrahydrofuran (0.3:3:0.5) is 12.6%.
    • (2) Para-phenylene diamine, hydrogenated tallowamine, sorbitol and carbamyl ethyl acetate at a mass ratio of 1:0.2:7:0.01 were taken, added to propyl alcohol, and stirred for one hour to obtain a mixed liquid II. The ratio of the total mass of the para-phenylene diamine, the hydrogenated tallowamine, the sorbitol and the carbamyl ethyl acetate to that of the propyl alcohol is 7.5%;
    • (3) The mixed liquid I obtained in step (1) was heated to 50° C., and the mixed liquid II obtained in step (2) was dripped at the speed of one drop per second, into the mixed liquid I obtained in step (1) with stirring and ultrasound, and heated to the temperature of 85° C. after the dripping is completed and the temperature was maintained for three hours while stopping stirring, and the temperature was decreased to the room temperature, so as to obtain a mixed liquid III. The mass ratio of the mixed liquid I to the mixed liquid II is 10:4.
    • (4) The mixed liquid III was added to an electrolytic cell with using a platinum electrode as an electrode and applying a voltage of 3 V to two ends of the electrode, and reacting for 13 minutes, to obtain a mixed liquid IV.
    • (5) The mixed liquid IV obtained in step (4) was heated with stirring, another mixed liquid II was taken and dripped into the mixed liquid IV obtained in step (4) at the speed of one drop per second. The mass ratio of the mixed liquid II to the mixed liquid IV is 1.05:1.25; and after the dripping is completed, the temperature was decreased to the room temperature under stirring, so as to obtain a mixed liquid V.
    • (6) A high-speed shearing treatment was performed on the mixed liquid V obtained in step (5) by using a high-speed shear mulser at the speed of 20000 revolutions per minute for one hour, so as to obtain a mixed liquid VI.
    • (7) Lyophilization treatment was performed on the mixed liquid VI to obtain a mixture I;
    • (8) The mixture I obtained in step (7) and absolute ethyl alcohol were mixed at a mass ratio of 1:2 and uniformly stirred, and were sealed at a temperature of 210° C. for performing solvent thermal treatment for 18 hours. The reaction was cooled to the room temperature, the obtained powder was collected by centrifugation, washed with deionized water and absolute ethyl alcohol eight times respectively, and dried to obtain a powder I.
    • (9) The powder I obtained in step (8) and ammonium persulfate was uniformly mixed at a mass ratio of 10:1, and sealed and heated to 165° C. The temperature was maintained for 13 hours. The reaction was cooled to the room temperature, the obtained mixed powder was washed with deionized water ten times, and dried to obtain a powder II.
    • (10) The powder II obtained in step (4) was placed into a crucible, heated to a temperature of 1500° C. at a speed of 3° C. per minute. The temperature was maintained for 7 hours. The reaction was cooled to the room temperature, to obtain an A-site high-entropy nanometer metal oxide (Gd0.4Er0.3La0.4Nd0.5Y0.4)(Zr0.7, Sn0.8, V0.5)O7 with high conductivity.

As observed via an electron microscope, the obtained A-site high-entropy nanometer metal oxide with high conductivity is a powder, and has microstructure of a square namometer sheet with a side length of about 4 nm and a thickness of about 1 nm.

The product powder was taken and compressed by using a powder sheeter at a pressure of 550 MPa into a sheet. Conductivity of the sheet is measured by using the four-probe method, and the conductivity of the product is 2.1×108 S/m.

A commercially available ITO (indium tin oxide) powder is taken and compressed by using a powder sheeter at a pressure of 550 MPa into a sheet, and the conductivity of the sheet is measured by using the four-probe method.

As measured, the conductivity of the commercially available ITO (indium tin oxide) is 1.6×106 S/m.

Patent 2024
1-Propanol 4-phenylenediamine Absolute Alcohol ammonium peroxydisulfate Cells Centrifugation Electric Conductivity Electrolytes Electron Microscopy Entropy Ethanol ethyl acetate Freeze Drying indium tin oxide Metals Molar Oxides Platinum Powder Pressure propyl acetate Solvents Sorbitol tetrahydrofuran Ultrasonography
Not available on PMC !

Example 6

ICP is monitored using a Samba 420 Sensor, pressure transducer, with a Samba 202 control unit (Harvard Apparatus, Holliston, MA). This ICP monitoring system consists of a 0.42 mm silicon sensor element mounted on an optical fiber. A 20-gauge syringe needle is implanted through the cisterna magna to a depth of ˜1 cm. The needle then acts as a guide for insertion of the Samba Sensor and the site of implantation and the open end of the needle are sealed with 100% silicone sealant. A baseline ICP reading is established followed by a water bolus IP injection (20% weight of animal) with or without Compound 1. ICP is monitored until the animal expires from the water load.

Adjusting for the slight rise in ICP observed in the animals when they are monitored without the water bolus injection (FIG. 9, No Water Toxicity), Compound 1 at 0.76 mg/kg reduces the relative rate of ICP rise by 36%, from 3.6×10−3 min−1 to 2.3×10−3 min−1 (n=6 mice/treatment, mean±SEM).

Patent 2024
Acceptance and Commitment Therapy Animals Injections, Intraperitoneal Intracranial Pressure Magna, Cisterna Mice, Laboratory Needles Ovum Implantation Silicon Silicones Syringes Transducers, Pressure

Example 1

Cell-free fractions were prepared as previously described (25). Briefly, Lactobacillus acidophilus strain La-5 was grown overnight in modified DeMann, Rogosa and Sharpe medium. (mMRS; 10 g peptone from casein, 8 g meat extract, 4 g yeast extract, 8 g D(+)-glucose, 2 g dipotassium hydrogen phosphate, 2 g di-ammonium hydrogen citrate, 5 g sodium acetate, 0.2 g magnesium sulfate, 0.04 g manganese sulfate in 1 L distilled water) (MRS; BD Diagnostic Systems, Sparks, MD). The overnight culture was diluted 1:100 in fresh medium. When the culture grew to an optical density at 600 nm (OD600) of 1.6 (1.2×108 cells/ml), the cells were harvested by centrifugation at 6,000×g for 10 min at 4° C. The supernatant was sterilized by filtering through a 0.2-μm-pore-size filter (Millipore, Bioscience Division, Mississauga, ON, Canada) and will be referred to as cell-free spent medium (CFSM). Two litres of L. acidophilus La-5 CFSM was collected and freeze-dried (Unitop 600 SL, VirTis Co., Inc. Gardiner, NY., USA). The freeze-dried CFSM was reconstituted with 200 ml of 18-Ω water. The total protein content of the reconstituted CFSM was quantified using the BioRad DC protein assay kit II (Bio-Rad Laboratories Ltd., Mississauga, ON, Canada). Freeze-dried CFSM was stored at −20° C. prior to the assays.

Patent 2024
ammonium citrate Biological Assay casein peptone Cells Centrifugation Diagnosis Freezing Glucose Hydrogen Lactobacillus acidophilus L Cells manganese sulfate Meat potassium phosphate, dibasic Proteins Sodium Acetate Sulfate, Magnesium Unitop Yeast, Dried

Top products related to «Water»

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TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.
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Methanol is a clear, colorless, and flammable liquid that is widely used in various industrial and laboratory applications. It serves as a solvent, fuel, and chemical intermediate. Methanol has a simple chemical formula of CH3OH and a boiling point of 64.7°C. It is a versatile compound that is widely used in the production of other chemicals, as well as in the fuel industry.
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C57BL/6J mice are a widely used inbred mouse strain. They are a commonly used model organism in biomedical research.
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TRIzol is a monophasic solution of phenol and guanidine isothiocyanate that is used for the isolation of total RNA from various biological samples. It is a reagent designed to facilitate the disruption of cells and the subsequent isolation of RNA.

More about "Water"

Water is a vital, ubiquitous substance that covers approximately 71% of the Earth's surface.
It is an essential component of life, serving as a crucial medium for numerous biological processes.
Water facilitates the transport of nutrients, regulates temperature, and enables essential chemical reactions.
In the field of water research, scientists and researchers explore the properties, distribution, and interactions of this fundamental resource.
Tools like the Milli-Q system, which produces high-purity water, and reagents such as TRIzol, methanol, formic acid, acetonitrile, DMSO, and sodium hydroxide, are commonly used in water-related experiments and analysis.
The study of water also intersects with other fields, such as the use of C57BL/6J mice, a common model organism, in water-based research.
Additionally, fetal bovine serum (FBS) is often utilized in cell culture experiments involving water-related processes.
PubCompare.ai is a powerful AI-driven platform that streamlines the workflow for water researchers.
It enables users to easily locate the best protocols from literature, preprints, and patents, while leveraging AI-driven comparisons to optimize reproducibility and identify the ideal products for water-related experiments.
This tool empowers researchers to take their water research to new heights, unlocking new discoveries and advancements in this critical domain.