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Calcium chloride

Calcium chloride is an inorganic compound with the chemical formula CaCl2.
It is a white, crystalline solid that is highly soluble in water and is commonly used as a desiccant, a de-icing agent, and in various industrial and medical applications.
Calcium chloride can also be used in research experiments, where it may be employed as a reagent or to modulate cellular processes.
PubCompare.ai's AI-driven platform can help researchers optimize their calcium chloride experiments by easily locating the best protocols from literature, preprints, and patents using intelligent comparisons.
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Most cited protocols related to «Calcium chloride»

1
Magnetic nanoparticle-based interstitial probes
Alginate probes were prepared using extrusion methods [18 (link)], [19 (link)]. Briefly, 1% sodium alginate in water functioned as the anionic solution and 2% calcium chloride containing 1% carboxymethylcellulose functioned as the cationic solution. Functionalized mNPs [12 ] (Micromod, 100 nm hydrodynamic diameter, iron oxide, dextran coated) were added to the cationic solution to achieve 1 mg/ml concentration. Droplets of the cationic solution were injected into 100 ml of anionic solution under constant stirring to generate hollow core beads. After alginate beads formed, they were rinsed with 2% calcium chloride three times, and incubated in 0.01% calcium solution at 4 °C. The resulting probes proved stable for two months. For spectroscopic measurements, calcium-alginated beads containing around 300 μg mNP were used.
We used blood as a surrogate for the interstitial in vivo environment. Blood contains most of the chemical complexities of the in vivo environment: the antibodies, enzymes, and a host of other proteins large and small present in vivo are all present in blood. Other biological samples are generally less problematic: urea, saliva, tissue, and so on. Blood is also the most commonly collected biological sample and has the most complicated composition. It has been shown that mNPs were readily taken in by cells resulting in a lower MSB signal [11 ]. Whole blood was harvested in an eppendorf tube containing heparin from the vena cava of euthanized C57BL/6 mice using a 3 mL syringe and a 25G needle. The whole blood was spun at 4500 r/min for 20 min at 4 °C, and the supernatant was used for experiments as plasma.
The spectroscopic measurements for the probe data were acquired at 1270 Hz on our original apparatus [9 ]–[12 ]. The ratio of the fifth over the third harmonics of the mNP magnetization was used as a concentration-independent metric [9 ], [10 (link)].
In the second arm of this paper, we tested the sensitivity of a recently introduced spectrometer that measures the magnetization perpendicular to the oscillating applied field. The perpendicular magnetization is induced by applying a small static field perpendicular to the oscillating applied field [20 (link)].
Zhang X., Reeves D., Shi Y., Gimi B., Nemani K.V., Perreard I.M., Toraya-Brown S., Fiering S, & Weaver J.B. (2015). Toward Localized In Vivo Biomarker Concentration Measurements. IEEE transactions on magnetics, 51(2), 1-4.
Publication 2015
Alginate Antibodies Biopharmaceuticals BLOOD Blood Substitutes Calcium, Dietary Calcium chloride Carboxymethylcellulose Cations Cells Dextran Enzymes ferric oxide Heparin Hydrodynamics Hypersensitivity Mice, Inbred C57BL Needles Plasma Saliva Sodium Alginate Spectrum Analysis Staphylococcal Protein A Syringes Tissues Urea Venae Cavae
2
Generating Pandemic Influenza Virus Variants
HA and NA genes for the Perth/2009 viral strain were cloned from recombinant virus obtained from BEI Resources (NR-41803) into the pHW2000 (79 (link)) influenza reverse-genetics plasmids to create pHW-Perth09-HA and pHW-Perth09-NA.
We initially created a virus with the HA and NA from Perth/2009 and internal genes from WSN/1933 and passaged it in cell culture to test its genetic stability. To generate this virus, we transfected a coculture of 293T and MDCK–SIAT1–TMPRSS2 in D10 media (DMEM, supplemented with 10% heat-inactivated FBS, or fetal bovine serum, 2 mM L-glutamine, 100 U of penicillin per milliliter, and 100 μ g of streptomycin per milliliter) with equal amounts of pHW-Perth09-HA, pHW-Perth09-NA, the pHW18 * series of plasmids (79 (link)) for all non-HA/NA viral genes, and pHAGE2–EF1aInt–TMPRSS2–IRES-mCherry-W. The next day, we changed the media to influenza growth media (IGM, consisting of Opti-MEM supplemented with 0.01% heat-inactivated FBS, 0.3% BSA, 100 U of penicillin per milliliter, 100 μ g of streptomycin per milliliter, and 100 μ g of calcium chloride per milliliter; no trypsin was added since there was TMPRSS2) and then collected the viral supernatant at 72 h posttransfection. This viral supernatant was blind passaged in MDCK–SIAT1–TMPRSS2 a total of six additional times. We isolated viral RNA from these passaged viruses and sequenced the HA gene. The passaged HA had two mutations, G78D and T212I, which enhanced viral growth as shown in SI Appendix, Fig. S1. The HA with these two mutations was cloned into pHW2000 (79 (link)) and pICR2 (80 (link)) to create pHW-Perth09-HA-G78D-T212I and pICR2-Perth09-HA-G78D-T212I. For all subsequent experiments, we used viruses with the HA containing these two mutations to improve titers and viral genetic stability, and this is the HA that we refer to as Perth/2009. We used all non-HA genes (including NA) from WSN/1933 to help increase titers and reduce biosafety concerns.
The codon-mutant libraries were generated using the approach in ref. 81 (link) with the modifications in ref. 82 (link). See SI Appendix, Supplementary Text for full details.
Lee J.M., Huddleston J., Doud M.B., Hooper K.A., Wu N.C., Bedford T, & Bloom J.D. (2018). Deep mutational scanning of hemagglutinin helps predict evolutionary fates of human H3N2 influenza variants. Proceedings of the National Academy of Sciences of the United States of America, 115(35), E8276-E8285.
Publication 2018
Blindness Calcium chloride Cell Culture Techniques Coculture Techniques Codon Culture Media Genes Genes, Viral Glutamine Influenza Internal Ribosome Entry Sites Mutation Penicillins Plasmids Reproduction RNA, Viral Strains Streptomycin TMPRSS2 protein, human Trypsin Virus
3
Optimizing Growth Conditions for M. extorquens
We first tested whether we could reliably measure M. extorquens exponential growth rates using a robotic measurement system under similar conditions to those used by previous investigators with E. coli[3] (link). AM1 cultures were grown in a Microtest 96-well tissue culture treated plates (Falcon-35-3072) using buffered medium comprised of 14.5 mM of K2HPO4, 18.8 mM of NaH2PO4, 8 mM ammonium sulfate, 20 µM calcium chloride and the C7 metal mix that was left unchelated (i.e., no citrate) with 17 mM methylamine·HCL added to the base medium. The mixture was aliquoted in 160 µL portions into wells of a 96-well plate. The growth curves from the initial tests in 96 well plates showed huge deviations from the exponential model and were exceptionally noisy. We concluded that 96-well plates were inadequate for sustained exponential growth of M. extorquens. We re-evaluated this conclusion at the end of this project, after optimizing our strains and media, by again growing M. extorquens in MP media and in 96-well plates (Fig S1). Although exponential growth could then be achieved, relative to a 48-well plate grown simultaneously with the same inoculum, the average estimated growth rate was 7% slower and the std. error was 50% larger.
In contrast, we found that 48-well plates did allow for adequate mixing and consistent exponential growth (Fig 1D). We therefore altered the robotic system by installing new custom-built racks so that it could use 48-well plates (CoStar-3548) instead of 96-well plates. In contrast to the 96-well plates where the medium did not appear to move within the well, the media in the 48-well plates rhythmically swirled around. We also tested a second type of 48-well plate, from the Cellstar line made by Greiner Bio-One (Catalog #677 102). Surprisingly, although medium in the CoStar plates visibly swirled while shaking, the meniscus in the Cellstar plates, as in the 96-well plates, stayed at approximately the same level and did not appear to move; correspondingly, cultures grew much more poorly in Cellstar plates. For all future work in this paper, we grew the cultures in CoStar plates in 640 µL per well with the incubator shaking at 650 RPM, as growth and the swirling of the liquid appeared to be as good or better than the range of other values tested.
Delaney N.F., Kaczmarek M.E., Ward L.M., Swanson P.K., Lee M.C, & Marx C.J. (2013). Development of an Optimized Medium, Strain and High-Throughput Culturing Methods for Methylobacterium extorquens. PLoS ONE, 8(4), e62957.
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Publication 2013
Calcium chloride Citrate Meniscus Metals methylamine potassium phosphate, dibasic Strains Sulfate, Ammonium Tissues
4
Isolation of Ribosomes from E. coli Strains
A fresh O/N culture of E. coli JE28 was used to inoculate 1 l. LB with 50 µg/ml kanamycin and grown with aeration at 37°C. At A600 1.0, the culture was slowly cooled to 4°C to produce run-off ribosome and harvested by centrifugation at 4000 rpm for 30 min. The cell-pellet was resuspended in lysis buffer (20 mM Tris–HCl pH 7.6, 10 mM MgCl2, 150 mM KCl, 30 mM NH4Cl and PMSF protease inhibitor 200 µl/l) with lysozyme (0.5 mg/ml) and DNAse I (10 µg/ml) and further lysed using a French Press or sonicator (for smaller cell pellets <2–3 g). The lysate was clarified by centrifuging twice at 18 000 rpm at 4°C, 20 min each. The cleared lysate was divided in half. From one-half 70S ribosome was purified in the conventional method and the affinity-purification method was employed with the other half. In parallel, wild-type ribosome was also purified from the parent strain MG1655 in the conventional way for comparison.
For affinity purification, a HisTrapTMHP column (Ni2+–sepharose pre-packed, 5 ml, GE Healthcare) was connected to an ÄKTA prime chromatography system (GE Healthcare) equilibrated with the lysis buffer. After loading the lysate, the column was washed with 5 mM imidazole until A260 reached the baseline. The tetra-(His)6-tagged ribosomes were then eluted with 150 mM imidazole, pooled immediately and dialyzed 4 × for 10 min in 250 ml lysis buffer to remove the imidazole. Furthermore, the ribosomes were concentrated by centrifugation at 150 000 × g for 2 h at 4°C, resuspended in 1× polymix buffer containing 5 mM ammonium chloride, 95 mM potassium chloride, 0.5 mM calcium chloride, 8 mM putrescine, 1 mM spermidine, 5 mM potassium phosphate and 1 mM dithioerythritol (23 (link)) and shock-frozen in liquid nitrogen for storage or dissolved in the overlay buffer (20 mM Tris–HCl pH 7.6, 60 mM NH4Cl, 5.25 mM Mg acetate, 0.25 mM EDTA and 3 mM 2-mercaptoethanol) for sucrose gradient analysis. As a control, lysate from wild-type E. coli MG1655 was applied to the same column and was treated accordingly.
For purifying JE28 and MG1655 ribosomes in the conventional ultracentrifugation method (24 (link)), the cleared lysate was layered on top of equal volume of 30% w/v sucrose cushion made in a buffer containing 20 mM Tris–HCl pH 7.6, 500 mM NH4Cl, 10.5 mM Mg acetate, 0.5 mM EDTA, and 7 mM 2-mercaptoethanol and centrifuged at 100 000 × g for 16 h at 4°C. This step was repeated twice and in between the ribosome pellet was gently rinsed with the same buffer. Then the pellet was dissolved in 1× polymix buffer for storage or in the overlay buffer for sucrose gradient analysis as in case of the affinity-purified ones.
Ederth J., Mandava C.S., Dasgupta S, & Sanyal S. (2008). A single-step method for purification of active His-tagged ribosomes from a genetically engineered Escherichia coli. Nucleic Acids Research, 37(2), e15.
Publication 2008
2-Mercaptoethanol Acetate Buffers Calcium chloride Cells Centrifugation Chloride, Ammonium Chromatography Chromatography, Affinity Deoxyribonuclease I Dithioerythritol Edetic Acid Escherichia coli Freezing imidazole Kanamycin Magnesium Chloride Muramidase Nitrogen Parent Pellets, Drug Potassium Chloride potassium phosphate Protease Inhibitors Putrescine Ribosomes Sepharose Shock Spermidine Strains Sucrose Tetragonopterus Tromethamine Ultracentrifugation
5
Optimized Choroidal Endothelial Cell Profiling
In order to more closely examine the transcriptome of choroidal endothelial cells, we modified our dissociation protocol prior to a second single-cell sequencing experiment to shift the distribution of analyzed cells to include more endothelial cells. In this experiment, separate 12-mm punches of RPE/choroid were centered on the macula and on the periphery (∼12 mm inferotemporal to the foveal center). Four human donors were included in this study (Table 1). Donors 5 to 7 had no documented ophthalmic history, while donor 4 had previously been diagnosed with neovascular AMD. After dissection away from the retina and sclera, the RPE/choroid was finely diced into small squares (∼1 × 1 mm) with a razor blade. The resulting suspension was dissociated in 450 units/mL collagenase II (Gibco) reconstituted in Hank’s balanced salt solution containing calcium chloride and magnesium chloride (Life Technologies) following a previously described protocol (65 (link)). RPE/choroid and collagenase II were incubated on a shaker at 37 °C for 1 h before cryopreservation, as described above.
Cryopreserved cells from donors 4 to 7 were rapidly thawed before preenrichment for endothelial cells. Cells were incubated for 15 min with anti-CD31 microbeads (Miltenyi Biotech) according to the manufacturer’s instructions before automated autoMACs magnetic separation (Miltenyi Biotech) of the CD31+ cell fraction. The positive cell fraction was passed 2 times through a 40-μm filter to remove aggregates. Single cells were immediately barcoded before library sequencing as described above. Cells with unique gene counts fewer than 500 were eliminated, and cells with more than 7,000 unique genes per cell were removed to eliminate potential doublets. Data were log-normalized before canonical correlation analysis aggregation was performed in Seurat.
Voigt A.P., Mulfaul K., Mullin N.K., Flamme-Wiese M.J., Giacalone J.C., Stone E.M., Tucker B.A., Scheetz T.E, & Mullins R.F. (2019). Single-cell transcriptomics of the human retinal pigment epithelium and choroid in health and macular degeneration. Proceedings of the National Academy of Sciences of the United States of America, 116(48), 24100-24107.
Publication 2019
Calcium Calcium chloride cDNA Library Cells Chlorides Choroid Collagenase Dissection Donors Endothelial Cells Endothelium Genes Homo sapiens Macula Lutea Magnesium Chloride Microspheres Pathologic Neovascularization Retina Sclera Sodium Chloride Tissue Donors Transcriptome Type II Mucolipidosis

Most recents protocols related to «Calcium chloride»

1
Antibody Reactivity Evaluation Across Species
Not available on PMC !

Example 3

Reactivity of the antibodies of the invention against several species of mesothelin (cyno, rat, mouse) was tested using assays well known in the art. The data is summarized in FIG. 4.

FACS binding assays were performed to evaluate the binding of the anti-Mesothlelin antibodies to murine, rat and cynomologous monkey mesothelin orthologues, using recombinant forms of the various receptors transiently expressed on 293T cells. FACs assays were performed by incubating hybridoma supernatants with 10,000 to 25,000 cells in PBS/2% Fetal bovine serum/2 mM Calcium Chloride at 4° C. for one hour followed by two washes with PBS/2% Fetal bovine serum/2 mM Calcium Chloride. Cells were then treated with florochrome-labeled secondary antibodies at 4° C. followed by one wash. The cells were resuspended in 50 μl of PBS/2% FBS and antibody binding was analyzed using a FACSCalibur™ instrument.

US11866508B2. Anti-mesothelin binding proteins (2024-01-09). AMGEN INC. [US]. Inventors: William Christian Fanslow, III [US], Carl Kozlosky [US], Jean Gudas [US].
Full text: Click here
Patent 2024
Anti-Antibodies Antibodies Biological Assay Calcium chloride Cells Cross Reactions HEK293 Cells Hybridomas Immunoglobulins Mesothelin Monkeys Mus
2
Hardening Fermented Liquid through pH Adjustment
Not available on PMC !

Example 3

Hardening of Fermented Liquid

Whey permeate that had been previously fermented and concentrated to form FACW was used to evaluate the impact on hardening time of adjusting pH with NH4(OH) and NaOH. The original pH of the FACW was 5.57 and 60% solids. Two pH levels were evaluated, pH 5.82 and 6.32, and they were set by using either NH4(OH) and NaOH to increase the pH of the FACW (4 treatments). For each of the four FACW treatments, 320 g was placed in a mixing bowl and mixing was initiated. Then 80 g of calcium chloride was slowly added over a total mixing time of 20 minutes. Subsequently, the mixture was poured into foil-lined trays and held at ambient temperature (74° F.). The mixtures were evaluated every 10 minutes for hardness. FACW which had pH adjusted to 5.82 and 6.32 reached a hard state by 90 and 60 minutes, respectively. In contrast, FACW that had pH adjusted with NaOH did not reach hardness. Results are presented in FIG. 1.

US11856969B2. Compositions and methods for solidified fermented animal feed (2024-01-02). PACKERLAND WHEY PRODUCTS [US]. Inventors: Tony Arnold [US], Michael De Veth [US], Aaron Hanke [US], Gerald Poppy [US], Brant Windham [US].
Full text: Click here
Patent 2024
ARID1A protein, human Calcium chloride Whey
3
pH Adjustment of Fermented Whey Permeate
Not available on PMC !

Example 5

Whey permeate that had been previously fermented and concentrated to form FACW was used to evaluate the impact on hardening time when adjusting to different pH with NH4(OH). The original pH of the FACW was 5.57 and solids of 60%. Two additional pH levels 5.82 and 6.32 were set by using NH4(OH) and evaluated. For each of the three pH levels, 320 g of FACW was placed in a mixing bowl and mixing was initiated. Then 80 g of calcium chloride was slowly added over a total mixing time of 20 minutes. Subsequently, the mixture was poured into foil-lined trays and held at cooled temperature (38° F.). The mixtures were evaluated every 10 minutes for hardness. FACW which had pH adjusted to 5.57, 5.82 and 6.32 reached a hard state by 60, 40 and 20 minutes, respectively. Results are presented in FIG. 3.

US11856969B2. Compositions and methods for solidified fermented animal feed (2024-01-02). PACKERLAND WHEY PRODUCTS [US]. Inventors: Tony Arnold [US], Michael De Veth [US], Aaron Hanke [US], Gerald Poppy [US], Brant Windham [US].
Full text: Click here
Patent 2024
ARID1A protein, human Calcium chloride Whey
4
Formulation and Preparation of Oil-Based Drilling Fluid
Not available on PMC !

Example 10

100 parts by weight of 3 #white oil and 6 parts by weight of an emulsifier (which was composed of 4 parts by weight of a primary emulsifier and 2 parts by weight of a secondary emulsifier) were taken and mixed at a stirring rate of 1,000 r/min for 10 min, 12 parts by weight of an organic clay was then added and blended at a stirring rate of 2,000 r/min for 10 min, 40 parts by weight of a calcium chloride aqueous solution (with a concentration of 25 wt %) was subsequently added and stirred at a stirring rate of 2,000 r/min for 10 min, 6 parts by weight of a wetting agent was further added and agitated at a stirring rate of 2,000 r/min for 10 min, 7 parts by weight of calcium oxide was then added and mixed at a stirring rate of 2,000 r/min for 20 min, 10 parts by weight of a filtrate reducer was subsequently added and blended at a stirring rate of 2,000 r/min for 20 min, 30 parts by weight of a weighting agent was further added and agitated at a stirring rate of 2,000 r/min for 20 min, 18 parts by weight of a plugging agent-S1 was subsequently added and stirred at a stirring rate of 2,000 r/min for 30 min, an oil-based drilling fluid (denoted as F10) was prepared.

The ingredients of F10 and contents thereof were shown in Table 1.

US11873444B1. Nanographene and preparation method and use thereof and oil-based drilling fluid (2024-01-16). Southwest Petroleum University [CN]. Inventors: Yang Bai [CN], Daoxiong Li [CN], Ren Wang [CN], Gang Xie [CN], Danchao Huang [CN], Wenzhe Li [CN], Feng Dai [CN], Jintang Wang [CN], Jing Zhang [CN], Jinsheng Sun [CN].
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Patent 2024
Calcium chloride calcium oxide Clay Wetting Agents
5
Bioceramic Composition Preparation Protocol
Not available on PMC !

Example 1

In the Bioceramic compositions 1 and 2 as described in Table 1, the solid components were firstly prepared in powder form using a planetary mixer in the following sequence: sorosilicate, radiopacifying agent and setting agent at speed below 400 rpm, about 30 minutes until complete homogenization. The aqueous liquid carrier was prepared using a mechanical stirrer and the components were added in the following sequence: water, accelerator agent and plasticizer at speed below 800 rpm, about 60 minutes until complete homogenization.

TABLE 1
Bioceramic compositions
Powder phaseAqueous liquid carrier
SampleSorosilicateRadiopacifierSetting agentVehicleAccelerator agentPlasticizer
CB 1AkermaniteCalciumCalcium sulfate/WaterCalcium chloridePolyvinyl
68%tungstatepotassium sulfate75%20%alcohol 5%
22%10%
CB 2BaghdaditeCalciumCalcium sulfate/WaterCalcium chloridePolyvinyl
68%tungstatepotassium sulfate75%20%alcohol 5%
22%10%

US11857558B2. Dental and medical compositions having a multiple source of metallic ions (2024-01-02). ANGELUS INDÚSTRIA DE PRODUTOS ODONTOLÓGICOS S/A [BR]. Inventors: César Eduardo Bellinati [BR], Cristiane Vila [BR], William Pereira Dos Santos [BR], Maíra Bendlin Calzavara [BR].
Full text: Click here
Patent 2024
akermanite Ca(3)ZrSi(2)O(9) Calcium chloride Calcium Sulfate carboranyl oligophosphate CB10 Chlorides Ethanol Plasticizers Polyvinyl Alcohol Polyvinyls Potassium Potassium Chloride potassium sulfate Powder Sulfates, Inorganic tungstate

Top products related to «Calcium chloride»

1
Calcium chloride by Merck Group
Sourced in United States, Germany, United Kingdom, India, Italy, Spain, China, France, Macao, Canada, Sao Tome and Principe, Switzerland, Belgium, Japan, Norway, Brazil, Singapore, Australia
Calcium chloride is a salt compound that is commonly used in various laboratory applications. It is a white, crystalline solid that is highly soluble in water. The core function of calcium chloride is to serve as a desiccant, absorbing moisture from the surrounding environment. It is also used as a source of calcium ions in chemical reactions and analyses.
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
Sodium alginate by Merck Group
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Sodium alginate is a naturally-derived, water-soluble polysaccharide that is commonly used as a thickening, stabilizing, and gelling agent in various laboratory applications. It is extracted from brown seaweed and is known for its ability to form viscous solutions and gels when combined with water. Sodium alginate is a versatile material that can be utilized in a range of laboratory procedures and formulations.
4
Potassium chloride (kcl) by Merck Group
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Potassium chloride (KCl) is an inorganic compound that is commonly used as a laboratory reagent. It is a colorless, crystalline solid with a high melting point. KCl is a popular electrolyte and is used in various laboratory applications.
5
Sodium hydroxide (naoh) by Merck Group
Sourced in Germany, United States, India, United Kingdom, Italy, China, Spain, France, Australia, Canada, Poland, Switzerland, Singapore, Belgium, Sao Tome and Principe, Ireland, Sweden, Brazil, Israel, Mexico, Macao, Chile, Japan, Hungary, Malaysia, Denmark, Portugal, Indonesia, Netherlands, Czechia, Finland, Austria, Romania, Pakistan, Cameroon, Egypt, Greece, Bulgaria, Norway, Colombia, New Zealand, Lithuania
Sodium hydroxide is a chemical compound with the formula NaOH. It is a white, odorless, crystalline solid that is highly soluble in water and is a strong base. It is commonly used in various laboratory applications as a reagent.
6
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.
7
Hydrochloric acid (hcl) by Merck Group
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Hydrochloric acid is a commonly used laboratory reagent. It is a clear, colorless, and highly corrosive liquid with a pungent odor. Hydrochloric acid is an aqueous solution of hydrogen chloride gas.
8
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.
9
Magnesium chloride by Merck Group
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Magnesium chloride is a chemical compound with the formula MgCl2. It is a white, crystalline solid that is highly soluble in water and other polar solvents. Magnesium chloride is a common laboratory reagent used in various applications.
10
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.

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