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> Chemicals & Drugs > Inorganic Chemical > Sodium Chloride

Sodium Chloride

Sodium chloride, also known as salt, is a chemical compound with the formula NaCl.
It is an essential mineral that plays a crucial role in maintaining the body's fluid balance, nerve function, and muscle contraction.
Sodium chloride is widely used in food processing, pharmaceutical applications, and industrial processes.
Researchers can utilize PubCompare.ai to optimize their sodium chloride research, locating the best protocols from literature, pre-prints, and patents, and improving reproducibility and accuracy through intelligent analysis.
This AI-enhanced research tool can help researchers experience the power of data-driven insights and streamline their sodium chloride studies.

Most cited protocols related to «Sodium Chloride»

1
RNA-seq Library Preparation from HEK293T Cells
Cited 1035 times
Nuclear RNA was prepared from HEK293T (kidney) cells. Briefly, cells were lysed on ice for 5 min in 10 mM Tris-HCl pH 7.5, 10 mM NaCl, 0.2 mM EDTA, 0.05% NP-40, and nuclei were spun at 2,500g for 3 min and then resuspended in QIAzol for RNA isolation using the miRNeasy kit according to the manufacturer’s instructions (Qiagen). The RNA-seq library was created using the Illumina TruSeq RNA Sample Preparation Kit v2 with the standard protocol, and sequenced on one lane of the HiSeq 2000 platform (100 bp, paired-end). Data are available at NCBI as accession number SRP041943. The database of annotated protein coding and noncoding genes (41,409 genes and 171,904 transcripts in total) was produced by merging all annotated genes from the RefSeq database29 (link), the UCSC Browser24 (link) and the Ensembl database30 (link).
Pertea M., Pertea G.M., Antonescu C.M., Chang T.C., Mendell J.T, & Salzberg S.L. (2015). StringTie enables improved reconstruction of a transcriptome from RNA-seq reads. Nature biotechnology, 33(3), 290-295.
Publication 2015
Cell Nucleus Cells DNA Library Edetic Acid Genes isolation Kidney Nonidet P-40 RNA, Nuclear RNA-Seq Sodium Chloride Standard Preparations Tromethamine
2
Protein-Protein Interaction Assay
Cited 566 times
Cells were solubilized with lysis buffer [50 mM Tris-HCl (pH7.5), 150 mM NaCl, 5 mM EDTA, 0.5% (v/v) NP-40, 50 mM NaF, 1 mM Na3VO4, 10 µg/ml leupeptin, 10 µg/ml aprotinin, 0.25 mM pAPMSF] and centrifuged at 12,000 × g for 20 min. For co-immunoprecipitation assay, cells were sonicated briefly in lysis buffer before centrifugation. The lysates were subjected to immunoprecipitation, SDS-PAGE, and Western blot analyses as described2 (link).
Nishita M., Park S.Y., Nishio T., Kamizaki K., Wang Z., Tamada K., Takumi T., Hashimoto R., Otani H., Pazour G.J., Hsu V.W, & Minami Y. (2017). Ror2 signaling regulates Golgi structure and transport through IFT20 for tumor invasiveness. Scientific Reports, 7, 1.
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Publication 2017
Aprotinin Biological Assay Buffers Cells Centrifugation Co-Immunoprecipitation Edetic Acid Immunoprecipitation leupeptin Nonidet P-40 SDS-PAGE Sodium Chloride Tromethamine Western Blot
3
Quantitative Proteomics of HeLa-E. coli Mixture
Cited 284 times
An Escherichia coli K12 strain was grown in standard LB medium, harvested, washed in PBS, and lysed in BugBuster (Novagen Merck Chemicals, Schwalbach, Germany) according to the manufacturer's protocol. HeLa S3 cells were grown in standard RPMI 1640 medium supplemented with glutamine, antibiotics, and 10% FBS. After being washed with PBS, cells were lysed in cold modified RIPA buffer (50 mm Tris-HCl, pH 7.5, 1 mm EDTA, 150 mm NaCl, 1% N-octylglycoside, 0.1% sodium deoxycholate, complete protease inhibitor mixture (Roche)) and incubated for 15 min on ice. Lysates were cleared by centrifugation, and after precipitation with chloroform/methanol, proteins were resuspended in 6 m urea, 2 m thiourea, 10 mm HEPES, pH 8.0. Prior to in-solution digestion, 60-μg protein samples from HeLa S3 lysates were spiked with either 10 μg or 30 μg of E. coli K12 lysates based on protein amount (Bradford assay). Both batches were reduced with dithiothreitol and alkylated with iodoacetamide. Proteins were digested with LysC (Wako Chemicals, GmbH, Neuss, Germany) for 4 h and then trypsin digested overnight (Promega, GmbH, Mannheim, Germany). Digestion was stopped by the addition of 2% trifluroacetic acid. Peptides were separated by isoelectric focusing into 24 fractions on a 3100 OFFGEL Fractionator (Agilent, GmbH, Böblingen, Germany) as described in Ref. 45 (link). Each fraction was purified with C18 StageTips (46 (link)) and analyzed via liquid chromatography combined with electrospray tandem mass spectrometry on an LTQ Orbitrap (Thermo Fisher) with lock mass calibration (47 (link)). All raw files were searched against the human and E. coli complete proteome sequences obtained from UniProt (version from January 2013) and a set of commonly observed contaminants. MS/MS spectra were filtered to contain at most eight peaks per 100 mass unit intervals. The initial MS mass tolerance was 20 ppm, and MS/MS fragment ions could deviate by up to 0.5 Da (48 (link)). For quantification, intensities can be determined alternatively as the full peak volume or as the intensity maximum over the retention time profile, and the latter method was used here as the default. Intensities of different isotopic peaks in an isotope pattern are always summed up for further analysis. MaxQuant offers a choice of the degree of uniqueness required in order for peptides to be included for quantification: “all peptides,” “only unique peptides,” and “unique plus razor peptides” (42 (link)). Here we chose the latter, because it is a good compromise between the two competing interests of using only peptides that undoubtedly belong to a protein and using as many peptide signals as possible. The distribution of peptide ions over fractions and samples is shown in supplemental Fig. S1.
Cox J., Hein M.Y., Luber C.A., Paron I., Nagaraj N, & Mann M. (2014). Accurate Proteome-wide Label-free Quantification by Delayed Normalization and Maximal Peptide Ratio Extraction, Termed MaxLFQ. Molecular & Cellular Proteomics : MCP, 13(9), 2513-2526.
Publication 2014
Acids Antibiotics, Antitubercular Biological Assay Buffers Cells Centrifugation Chloroform Cold Temperature Deoxycholic Acid, Monosodium Salt Digestion Dithiothreitol Edetic Acid Escherichia coli Escherichia coli K12 Glutamine HeLa Cells HEPES Homo sapiens Immune Tolerance Iodoacetamide Ions Isotopes Liquid Chromatography Methanol Peptides Promega Protease Inhibitors Proteins Proteome Radioimmunoprecipitation Assay Retention (Psychology) Sodium Chloride Staphylococcal Protein A Tandem Mass Spectrometry Thiourea Tromethamine Trypsin Urea
4
Alanine Dipeptide Conformational Analysis
Cited 231 times
The alanine dipeptide was built with YASARA,21 adding acetyl‐ and N‐methyl capping groups. The system consisted of ∼3000 atoms (32 peptide atoms, 981 water molecules, and three ion pairs, that is, 0.98% NaCl). The force field was AMBER03, simulations were run at 298 K with the protocols described in the caption of Figure 6. After an equilibration period of 1 ns, the current φ/ψ dihedrals were calculated every 50 fs and mapped to a two‐dimensional grid with a resolution of 5° (72 × 72 bins), then the corresponding counter was incremented. After a microsecond, the probability in each grid bin was obtained by dividing with the total number of counts, converted to a free energy using the well known Boltzmann formula Energy = −BoltzmannConstant × 298 × ln(Probability), shifted so that the energy minimum was at 0, and visualized using the marching squares algorithm for seven contour levels with a spacing of 4 kJ/mol. The YASARA macro used to perform these tasks can be found in the documentation of the free YASARA View program version 15 or later, at Commands > Options > Tables > Tabulate.
Krieger E, & Vriend G. (2015). New ways to boost molecular dynamics simulations. Journal of Computational Chemistry, 36(13), 996-1007.
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Publication 2015
Alanine Dipeptides Peptides Sodium Chloride
5
Bacterial Cell Culture and Genetic Manipulation
Cited 190 times
Cells were routinely grown in LB medium containing 1% Bacto Tryptone (Difco), 0.5% yeast extract (Difco), and 0.5% NaCl with or without antibiotics at 50 μg/ml for ampicillin (Wako, Osaka, Japan) and 30 μg/ml for kanamycin (Wako, Osaka, Japan). Glucose, L-arabinose, and other chemicals were from Wako (Osaka, Japan). DpnI was from New England Biolabs (MA, USA); Taq polymerase, TaKaRa Ex Taq, and agarose, SeaKem GTG Agarose from Takara Shuzo Inc. E-Gel 96 systems were from Invitrogen. MOPS medium was prepared as described elsewhere (Wanner, 1994 ).
Baba T., Ara T., Hasegawa M., Takai Y., Okumura Y., Baba M., Datsenko K.A., Tomita M., Wanner B.L, & Mori H. (2006). Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Molecular Systems Biology, 2, 2006.0008.
Publication 2006
Ampicillin Antibiotics, Antitubercular Arabinose Cells Glucose Kanamycin morpholinopropane sulfonic acid Sepharose Sodium Chloride Taq Polymerase Yeast, Dried

Most recents protocols related to «Sodium Chloride»

1
Purification of IL-2 Mutein Polymer Prodrug
Not available on PMC !

Example 6

Compound 3 was generated from the purification process of IL-2 mutein Ala-M1 polymer prodrug 5. During separation of compound 5 on a Capto MMC ImpRes resin the later eluting peak which contains 3 was collected. The collected fraction was diluted with 10 mM succinic acid, pH 5.0 to lower the conductivity to approx. 14 mS/cm and further purified on a Äkta system equipped with a HiScreen Capto Blue column using buffer A (20 mM sodium phosphate, pH 7.5), buffer B (20 mM sodium phosphate, 1 M NaCl, pH 7.5) and a gradient from 0 to 50% buffer B in 6 column volumes. The main peak was collected and concentrated using Amicon Ultra centrifugal device (3 kDa MWCO). The concentrated solution was buffer exchanged to 10 mM Hepes, 150 mM NaCl, 3 mM EDTA, 0.05% polysorbate 20, pH 7.4 by using an Äkta system and a HiPrep 26/10 column and the concentration was adjusted to 0.25 mg/mL to give compound 3.

US11879001B2. Conjugate comprising an IL-2 moiety (2024-01-23). ASCENDIS PHARMA ONCOLOGY DIVISION A/S [DK]. Inventors: Nina Gunnarsson [DK], Matiss Maleckis [DK], David B. Rosen [US].
Full text: Click here
Patent 2024
Buffers Edetic Acid Electric Conductivity HEPES interleukin-2, polyethylene glycol-modified Medical Devices mutein 2 mutein 5 Polymers Polysorbate 20 Prodrugs Resins, Plant Sodium Chloride sodium phosphate Succinic Acid
2
Enhanced Absorbency of Embossed SAM Sheets
Not available on PMC !

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.

US11864985B2. Absorbent composites containing embossed superabsorbent materials (2024-01-09). Kimberly-Clark Worldwide, Inc. [US]. Inventors: Feng Chen [US], Wing-Chak Ng [US], Mark M. Mleziva [US].
Full text: Click here
Patent 2024
acrylate Convection Electroplating Metals Molecular Structure Muscle Rigidity Polymers Pressure Retention (Psychology) Saline Solution SKAP2 protein, human Sodium Chloride Urination
3
Synthetic Urine-based Electrochemical Biosensor for Urine Albumin Detection
Not available on PMC !

Example 7

Synthetic urine is prepared by dissolving 14.1 g of NaCl, 2.8 g KCl, 17.3 g of urea, 19 ml ammonia water (25%), 0.60 g CaCl2 and 0.43 g MgSO4 in 0.02 mole/L of HCl. The final pH of synthetic urine is adjusted to 6.04 by using HCl and ammonia water.

40 mg Sigma creatinine is dissolved in 10 ml of synthetic urine solution. 3 mg of human albumin is dissolved in 10 ml of synthetic urine solution to prepare the micro albumin solution.

4 mg Sigma hemin is dissolved in 20 ml of synthetic urine, 20 μL Hemin solution is used as a receptor for urine albumin detection at different creatinine concentration.

A desired volume of the biological sample (synthetic urine) is taken and dispensed on the electrode of the biosensor device and the corresponding cyclic voltammogram is obtained by the CHI-Electrochemical workstation using the potential window, that varies from 0 V to −1 V with scan rate of 0.1 V/sec.

The albumin content in the urine sample binds hemin thereby demonstrates a linear decrease in peak redox current with urine albumin concentration as shown in FIG. 15(a) for different creatinine concentrations. If the concentration of albumin in urine sample is increased, then the albumin increasingly binds with hemin thereby reducing the free hemin concentration on the electrode resulting in the decrease in peak redox current of free hemin. FIG. 16 shows the urine albumin concentrations, urine creatinine concentrations and calculated ACR for different samples.

The values of concentrations of the urine albumin (mg/L) and creatinine for different samples is shown in Table 4.

TABLE 4
SampleUrine albuminUrine CreatinineACR
Number(mg/L)(mg/dL)(mg/g)
1526.719
22026.775
35026.7187
410026.7375
515026.7562
65133.34
720133.315
850133.338
9100133.375
10150133.3113

US11867654B2. Device and method for detecting creatinine and albumin to creatinine ratio (2024-01-09). INDIAN INSTITUTE OF SCIENCE [IN]. Inventors: Vinay Kumar [IN], Navakanta Bhat [IN], Nikhila Kashyap Dhanvantari Madhuresh [IN].
Full text: Click here
Patent 2024
Albumins Ammonium Hydroxide Biopharmaceuticals Biosensors Creatinine Hemin Moles Oxidation-Reduction Radionuclide Imaging Receptors, Albumin Serum Albumin, Human Sodium Chloride Sulfate, Magnesium Urea Urine
4
Purification and Immobilization of FC4E Enzyme for Tagatose Production
Not available on PMC !

Example 9

NEBT7EL-pA06238 was grown on LB with 50 μg/ml kanamycin. A 600 ml culture of TBkan50 was inoculated with NEBT7EL-pA06238 and incubated overnight at 37° C. at 200 rpm. The next morning, a 10 L fermentor was prepared with 9.5 L of TB and then inoculated with 500 ml of the overnight culture. The culture was grown at 37° C. The pH was maintained at 6.2 with NaOH and the dO2 was maintained ≥20%. After 2 hours of growth, the temperature was dropped to 25° C. The culture was grown for an additional 1 hour with the OD600 around 7. IPTG was added to a final concentration of 1 mM and CoCl2 was added to 25 μM. Additional CoCl2 was added 1 and 2 hours after induction to bring the final concentration to 300 μM. The cells were grown for 20 hours at which point the fermentor was chilled to 10° C. and the cells were harvested by centrifugation. The cell pellet was stored at −80° C. until use.

The cell pellet from the fermentation was lysed by stirring in buffer with lysozyme and DNAse. Cell debris was removed by centrifugation and the supernatant was filtered through a 0.45 micron filter. Filtered supernatant was incubated with Ni-NTA agarose resin and then enzyme was eluted with imidazole. Purified FC4E pA06238 was immobilized onto 5.25 grams of ECR8204F resin using the standard published protocol from Purolite.

The immobilized enzyme was loaded into a 11×300 mm glass fixed bed reactor and run for approximately 200 h at constant temperature (60° C.) with a constant feed composition of 30 wt % fructose+70 wt % aqueous buffer solution (20 mM KPO4, 50 mM NaCl, 300 uM CoCl2). Feed rate was held constant at 140 uL/min throughout the run. The fixed bed reaction reached a maximal conversion of approximately 30% tagatose and had a half-life of −50 hours (FIG. 15).

US11866758B2. Methods and compositions for preparing tagatose from fructose (2024-01-09). Arzeda Corp. [US]. Inventors: Alexandre Zanghellini [US], Kyle Roberts [US], Michael Charles Milner Cockrem [US], Christopher Dunckley [US].
Full text: Click here
Patent 2024
ARID1A protein, human Buffers Cells Centrifugation Deoxyribonucleases Enzymes Enzymes, Immobilized Fermentation Fermentors Fructose imidazole Isopropyl Thiogalactoside Kanamycin Muramidase Resins, Plant Sepharose Sodium Chloride tagatose
5
Synthesis of 5-Iodo-6-Methyl Pyrimidine Dione Derivative
Not available on PMC !

Example 1

10 g (33.09 mmol) of 1-(2-fluoro-6-trifluoromethyl-benzyl)-6-methyl-1H-pyrimidine-2,4-dione (III), 6.8 g (49.62 mmol) of K2CO3 and 2.4 g (6.6 mmol) of tetrabutylammonium iodide were mixed with 50 mL of acetone at the temperature of about 20° C. Subsequently, 13.6 g (43.12 mmol) of (R)-2-((tert-butoxycarbonyl)amino)-2-phenylethyl methanesulfonate (IVa) were added and the obtained mixture was heated at the temperature of about 55° C. and maintained under stirring for about 16 hours at said temperature.

Once this maintenance was finished, the solvent was vacuum distilled and 50 mL of ethyl acetate and 50 mL of water were added to the residue thus obtained. A 1 M aqueous solution of HCl was slowly added, maintaining the temperature between 20 and 25° C. until achieving a pH of between 7 and 8. The aqueous phase was separated and treated with 3 fractions of 30 mL each of ethyl acetate. All the organic extracts were pooled and the solvent was removed by means of vacuum to obtain a slightly yellowish oily residue to which 45 mL of methanol were added, obtaining complete dissolution of the residue.

Example 2

16.1 g (99.24 mmol) of iodine monochloride (ICI) were dissolved in 40 mL of methanol at the temperature of about 10° C. The methanol solution previously obtained according to the methodology described in Example 1 comprising 3-((R)-2-(tert-butoxycarbonyl)amino-2-phenylethyl)-1-(2-fluoro-6-trifluoromethylbenzyl)-6-methyl-1H-pyrimidine-2,4-dione (II) was added to the iodine monochloride solution, maintaining the temperature between 20 and 25° C. Once the addition was finished, the obtained solution was heated to about 50° C. and was maintained under stirring for 2 hours at the mentioned temperature.

Once the maintenance was finished, the solvent was vacuum distilled and 50 mL of acetone were slowly added to the obtained oily residue at the temperature of between and 25° C. The addition of acetone caused a solid precipitate to appear almost immediately. The obtained mixture was maintained for 1 hour under stirring at the mentioned temperature. The resulting solid was isolated by filtration, washed with two fractions of 25 mL of acetone, and finally dried at the temperature of 50° C. to obtain 15.6 g (80.8% yield) of a white solid corresponding to the 3-((R)-2-(amino-2-phenylethyl)-1-(2-fluoro-6-trifluoromethylbenzyl)-5-iodo-6-methyl-1H-pyrimidine-2,4-dione hydrochloride salt (Ia) (UHPLC purity: 98.9%).

1H-NMR (d6-DMSO, 400 MHz) δ (ppm): 8.70 (2H, s broad), 7.65-7.48 (3H, m), 7.40-7.32 (5H, m), 5.40-5.29 (2H, dd), 4.47 (1H, t), 4.25 (2H, dd), 2.65 (3H, s).

13C-NMR (d6-DMSO, 100 MHz) δ (ppm): 161.87, 159.47, 159.41, 154.19, 150.98, 134.70, 129.93, 129.84, 129.01, 128.58, 127.38, 122.61, 122.34, 122.22, 121.34, 121.10, 74.80, 52.26, 45.45, 44.60, 25.66.

The DSC of this compound is shown in FIG. 1 and the XRPD is shown in FIG. 2.

US11858901B2. 3-((R)-2-(amino-2-phenylethyl)-1-(2-fluoro-6 trifluoromethyl benzyl)-5-iodo-6-methyl-1H-pyrimidine-2,4-dione or a salt thereof, process for its preparation, and its use in the synthesis of elagolix (2024-01-02). MOEHS IBERICA, S.L. [ES]. Inventors: Roberto Ballette [ES], Oscar Jiménez Alonso [ES], Elena García García [ES], Alicia Dobarro Rodríguez [ES].
Full text: Click here
Patent 2024
1H NMR Acetone Anabolism Carbon-13 Magnetic Resonance Spectroscopy elagolix ethyl acetate Filtration Iodine iodine monochloride methanesulfonate Methanol Oils potassium carbonate Pyrimidines Sodium Chloride Solvents Sulfoxide, Dimethyl TERT protein, human tetrabutylammonium iodide Vacuum

Top products related to «Sodium Chloride»

1
Protease inhibitor cocktail by Roche
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Protease inhibitor cocktail is a laboratory reagent used to inhibit the activity of proteases, which are enzymes that break down proteins. It is commonly used in protein extraction and purification procedures to prevent protein degradation.
2
Sodium chloride (nacl) by Merck Group
Sourced in United States, Germany, United Kingdom, India, Italy, France, Spain, China, Canada, Sao Tome and Principe, Poland, Belgium, Australia, Switzerland, Macao, Denmark, Ireland, Brazil, Japan, Hungary, Sweden, Netherlands, Czechia, Portugal, Israel, Singapore, Norway, Cameroon, Malaysia, Greece, Austria, Chile, Indonesia
NaCl is a chemical compound commonly known as sodium chloride. It is a white, crystalline solid that is widely used in various industries, including pharmaceutical and laboratory settings. NaCl's core function is to serve as a basic, inorganic salt that can be used for a variety of applications in the lab environment.
3
Protease inhibitor cocktail by Merck Group
Sourced in United States, Germany, China, United Kingdom, Italy, Japan, Sao Tome and Principe, France, Canada, Macao, Switzerland, Spain, Australia, Israel, Hungary, Ireland, Denmark, Brazil, Poland, India, Mexico, Senegal, Netherlands, Singapore
The Protease Inhibitor Cocktail is a laboratory product designed to inhibit the activity of proteases, which are enzymes that can degrade proteins. It is a combination of various chemical compounds that work to prevent the breakdown of proteins in biological samples, allowing for more accurate analysis and preservation of protein integrity.
4
Pvdf membrane by Merck Group
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PVDF membranes are a type of laboratory equipment used for a variety of applications. They are made from polyvinylidene fluoride (PVDF), a durable and chemically resistant material. PVDF membranes are known for their high mechanical strength, thermal stability, and resistance to a wide range of chemicals. They are commonly used in various filtration, separation, and analysis processes in scientific and research settings.
5
Complete protease inhibitor cocktail by Roche
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The Complete Protease Inhibitor Cocktail is a laboratory product designed to inhibit a broad spectrum of proteases. It is a concentrated solution containing a mixture of protease inhibitors effective against a variety of protease classes. This product is intended to be used in research applications to preserve the integrity of target proteins by preventing their degradation by proteolytic enzymes.
6
Bovine serum albumin (bsa) by Merck Group
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
7
Fetal bovine serum (fbs) by Thermo Fisher Scientific
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
8
Protease inhibitor by Roche
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Protease inhibitors are a class of laboratory equipment used in the field of biochemistry and molecular biology. These inhibitors are designed to specifically target and inactivate proteases, which are enzymes that break down proteins. Protease inhibitors play a crucial role in various experimental and analytical procedures, such as protein extraction, purification, and stabilization.
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Pierce bca protein assay kit by Thermo Fisher Scientific
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The Pierce BCA Protein Assay Kit is a colorimetric-based method for the quantification of total protein in a sample. It utilizes the bicinchoninic acid (BCA) reaction, where proteins reduce Cu2+ to Cu+ in an alkaline environment, and the resulting purple-colored reaction is measured spectrophotometrically.
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Dimethyl sulfoxide (dmso) by Merck Group
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DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.

More about "Sodium Chloride"

Sodium chloride, also known as salt (NaCl), is a crucial mineral with diverse applications.
It plays a vital role in maintaining the body's fluid balance, nerve function, and muscle contraction, making it an essential nutrient.
In research, sodium chloride is widely used in various applications, including food processing, pharmaceutical formulations, and industrial processes.
Researchers can leverage the power of AI-driven tools like PubCompare.ai to optimize their sodium chloride studies.
This intelligent platform allows researchers to locate the best protocols from literature, preprints, and patents, enhancing the reproducibility and accuracy of their experiments.
By utilizing PubCompare.ai, researchers can experience the benefits of data-driven insights, streamlining their sodium chloride research and unlocking new possibilities.
Closely related to sodium chloride are other important research tools and compounds, such as protease inhibitor cocktails, PVDF membranes, bovine serum albumin (BSA), and the Pierce BCA Protein Assay Kit.
These materials often work in conjunction with sodium chloride-based protocols, providing a comprehensive toolset for researchers studying various biological and chemical processes.
Additionally, the use of dimethyl sulfoxide (DMSO) can be relevant in sodium chloride research, as it is a versatile solvent commonly used in cell-based studies and pharmaceutical applications.
By understanding the interconnectedness of these related terms and concepts, researchers can develop a more holistic understanding of the sodium chloride research landscape and optimize their investigations accordingly.