The gating current measurements were performed on a cut-open oocyte voltage clamp set-up (CA-1B; Dagan Corporation) as described previously (Muroi et al., 2010 (link); Lacroix and Bezanilla, 2011 (link)). For the potassium channel gating current measurement, the external solution was 115 mM NMG-MES (N-methyl-d -glucamine methanesulfonate), 2 mM Ca-MES, and 10 mM Hepes, pH 7.4. For the sodium channel gating current measurement, the external solution was 115 mM Na-MES, 2 mM Ca-MES, and 10 mM Hepes, pH 7.4. In the latter case, all ionic currents were blocked by the application of 10 µM tetrodotoxin to the external and middle chambers. For both channels, the internal solution was 115 mM NMG-MES, 2 mM EGTA, and 10 mM Hepes, pH 7.4. The recording pipette resistance was 0.3–0.5 MΩ. Analogue signals were sampled at 250 kHz with a Digidata 1440 interface (Molecular Devices) and low-pass filtered at 10 kHz. The capacitive transient currents were subtracted online using the P/4 method with a subtraction holding potential of −120 mV for the potassium channels and 50 mV for the sodium channels. Gating currents were obtained by applying a depolarizing pulse (50 ms for potassium and 20 ms for sodium channels) to voltages from −120 to 10 mV (at 5-mV intervals) for the potassium channels and −160 to 30 mV (at 10-mV intervals) for the sodium channels. The holding potential was −90 mV, and a 50-ms-long pre- and postpulse at −130 mV was used.
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Sodium-20
Sodium-20
Sodium-20 is a radioisotope of sodium with a half-life of approximately 17.8 seconds.
It is used in various research applications, including medical imaging, tracer studies, and nuclear physics experiments.
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It is used in various research applications, including medical imaging, tracer studies, and nuclear physics experiments.
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Most cited protocols related to «Sodium-20»
Dagan
Egtazic Acid
HEPES
Ion Transport
Medical Devices
methanesulfonate
Oocytes
Potassium-50
Potassium Channel
Pulse Rate
Sodium-20
Sodium Channel
Subtraction Technique
Tetrodotoxin
Transients
Colonic luminal content samples were weighed into 1.5 ml tubes, crushed and homogenized in 100 µl of distilled water. Subsequently, 40 mg of sodium chloride, 20 mg of citric acid, 40 µl of 1 M hydrochloric acid, and 200 µl of butanol were added. The tubes were vortexed for 2 min and centrifuged at 18,000×g for 15 min. The supernatant was transferred to microtubes, and 1 µl was injected into the gas chromatograph. For serum measurements, 20 mg of sodium chloride, 10 mg of citric acid, 20 µl of 1 M hydrochloric acid, and 100 µl of butanol were added to 100 µl of serum samples. Tubes were vortexed and centrifuged as previously described and 1 µl was injected into the gas chromatograph. To quantify SCFAs, a calibration curve for the concentration range of 0.015–1 mg/ml was constructed. SCFAs measurements were performed following a recently published protocol41 (link): chromatographic analyses were performed using an Agilent 6850 system with ExChrom software, equipped with a 7683B automatic liquid sampler, a flame ionization detector (FID) (Agilent Technologies, USA), and a fused-silica capillary RTX-WAX (Restec Corporation, U.S.) with dimensions of 60 m × 0.25 mm internal diameter (i.d.) coated with a 0.15-µm thick layer of polyethylene glycol. The initial oven temperature was 100 °C (hold 2 min), which was increased to 200 °C at a rate of 15 °C/min (hold 5 min). The FID temperature was maintained at 260 °C, and the flow rates of H2, air, and the make-up gas N2 were 35, 350, and 25 ml/min, respectively. Sample volumes of 1 µl were injected at 260 °C using a split ratio of approximately 25:1. Nitrogen was used as the carrier gas at 25 ml/min. The runtime for each analysis was 12.95 min.
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Butyl Alcohol
Capillaries
Chlorides
Chromatography
Citric Acid
Colon
Flame Ionization
Gas Chromatography
Hydrochloric acid
Nitrogen
Phenobarbital
Polyethylene Glycols
Serum
Silicon Dioxide
Sodium-20
Sodium Chloride
Amylin
Buffers
cysteinylcysteine
Disulfides
hexafluoroisopropanol
Homo sapiens
Isotopes
Peptides
Phosphates
Sodium-20
Sodium Chloride
sodium phosphate
Solvents
697 B-ALL cells
and Molm-14 AML cells were cultured in the presence of11 or vehicle-only for 1.0 h. Pervanadate solution was prepared fresh
by combining 20 mM sodium orthovanadate in 0.9× PBS in a 1:1
ratio with 0.3% (w/w) hydrogen peroxide in PBS for 15–20 min
at room temperature. Cultures were treated with 120 μM pervanadate
for 3 min prior to collection, and cell lysates were prepared in 50
mM HEPES (pH 7.5), 150 mM NaCl, 10 mM EDTA, 10% glycerol, and 1% Triton
X-100, supplemented with protease inhibitors (Roche Molecular Biochemicals,
no. 11836153001). Mer and Flt3 proteins were immunoprecipitated with
anti-Mer (R&D Systems, no. MAB8912) or anti-Flt3 (Santa Cruz Biotechnology
no. sc-480) antibody and Protein G agarose beads (InVitrogen). Phospho-proteins
were detected by Western blot using an antiphospho-Mer antibody raised
against a peptide derived from the triphosphorylated activation loop
of Mer8 (link) (Phopshosolutions, Inc.) or an
antibody specific for phosphorylated Flt3 (Cell Signaling Technology,
no. 3461). Nitrocellulose membranes were stripped and total proteins
were detected using a second anti-Mer antibody (Epitomics Inc., no.
1633-1) or anti-Flt3 antibody (Santa Cruz Biotechnology no. sc-480).
Relative phosphorylated and total protein levels were determined by
densitometry using ImageJ, and IC50 values were calculated
by nonlinear regression.
32D Cells expressing a chimeric EGFR-Mer,
EGFR-Axl, or EGFR-Tyro3 receptor were cultured in the presence of11 or vehicle-only for 1.0 h before stimulation with 100 ng/mL
EGF (BD Biosciences no. 354010) for 15 min. Cells were centrifuged
at 1000g for 5 min and washed with 1× PBS. Cell
lysates were prepared in 20 mM HEPES (pH 7.5), 50 mM NaF, 500 mM NaCl,
5.0 mM EDTA, 10% glycerol, and 1% Triton X-100, supplemented with
protease inhibitors (10 μg/mL leupeptin, 10 μg/mL phenylmethylsulfonyl
fluoride, and 20 μg/mL aprotinin) and phosphatase inhibitors
(50 mM NaF and 1.0 mM sodium orthovanadate). Mer protein was immunoprecipitated
using a custom polyclonal rabbit antisera raised against a peptide
derived from the C-terminal catalytic domain of Mer and Protein A
agarose beads (Santa Cruz Biotechnology). Axl and Tyro3 proteins were
immunoprecipitated using an antibody directed against a FLAG epitope
engineered into the chimeric proteins (Sigma-Aldrich, no. F1804).
Phosphotyrosine-containing proteins were detected by Western blot
with a monoclonal HRP-conjugated antiphosphotyrosine antibody (Santa
Cruz Biotechnology, no. sc-508). Antibodies were stripped from membranes,
and total proteins were detected with the same antibodies used for
immunoprecipitation.
and Molm-14 AML cells were cultured in the presence of
by combining 20 mM sodium orthovanadate in 0.9× PBS in a 1:1
ratio with 0.3% (w/w) hydrogen peroxide in PBS for 15–20 min
at room temperature. Cultures were treated with 120 μM pervanadate
for 3 min prior to collection, and cell lysates were prepared in 50
mM HEPES (pH 7.5), 150 mM NaCl, 10 mM EDTA, 10% glycerol, and 1% Triton
X-100, supplemented with protease inhibitors (Roche Molecular Biochemicals,
no. 11836153001). Mer and Flt3 proteins were immunoprecipitated with
anti-Mer (R&D Systems, no. MAB8912) or anti-Flt3 (Santa Cruz Biotechnology
no. sc-480) antibody and Protein G agarose beads (InVitrogen). Phospho-proteins
were detected by Western blot using an antiphospho-Mer antibody raised
against a peptide derived from the triphosphorylated activation loop
of Mer8 (link) (Phopshosolutions, Inc.) or an
antibody specific for phosphorylated Flt3 (Cell Signaling Technology,
no. 3461). Nitrocellulose membranes were stripped and total proteins
were detected using a second anti-Mer antibody (Epitomics Inc., no.
1633-1) or anti-Flt3 antibody (Santa Cruz Biotechnology no. sc-480).
Relative phosphorylated and total protein levels were determined by
densitometry using ImageJ, and IC50 values were calculated
by nonlinear regression.
32D Cells expressing a chimeric EGFR-Mer,
EGFR-Axl, or EGFR-Tyro3 receptor were cultured in the presence of
EGF (BD Biosciences no. 354010) for 15 min. Cells were centrifuged
at 1000g for 5 min and washed with 1× PBS. Cell
lysates were prepared in 20 mM HEPES (pH 7.5), 50 mM NaF, 500 mM NaCl,
5.0 mM EDTA, 10% glycerol, and 1% Triton X-100, supplemented with
protease inhibitors (10 μg/mL leupeptin, 10 μg/mL phenylmethylsulfonyl
fluoride, and 20 μg/mL aprotinin) and phosphatase inhibitors
(50 mM NaF and 1.0 mM sodium orthovanadate). Mer protein was immunoprecipitated
using a custom polyclonal rabbit antisera raised against a peptide
derived from the C-terminal catalytic domain of Mer and Protein A
agarose beads (Santa Cruz Biotechnology). Axl and Tyro3 proteins were
immunoprecipitated using an antibody directed against a FLAG epitope
engineered into the chimeric proteins (Sigma-Aldrich, no. F1804).
Phosphotyrosine-containing proteins were detected by Western blot
with a monoclonal HRP-conjugated antiphosphotyrosine antibody (Santa
Cruz Biotechnology, no. sc-508). Antibodies were stripped from membranes,
and total proteins were detected with the same antibodies used for
immunoprecipitation.
Antibodies
Antibodies, Anti-Idiotypic
Aprotinin
Catalytic Domain
Cells
Chimera
Edetic Acid
EGFR protein, human
FLT3 protein, human
G-substrate
Glycerin
HEPES
Immune Sera
Immunoglobulins
inhibitors
Intestinal Atresia, Multiple
leupeptin
Monoclonal Antibodies
Nitrocellulose
Orthovanadate
Peptides
Peroxide, Hydrogen
pervanadate
Phosphoric Monoester Hydrolases
Phosphotyrosine
Protease Inhibitors
Proteins
Rabbits
Sepharose
Sodium
Sodium-20
Sodium Chloride
Tissue, Membrane
Triton X-100
Western Blotting
RAD51 mouse monoclonal and horseradish peroxidase- or Alexa-Fluor 488-labeled secondary antibodies were purchased and provided to the Tissue Core Facility of the Karmanos Cancer Institute. The tissue core facility used these antibodies to evaluate the expression of RAD51 in the specimens of human esophagi, under approved Institutional Review Board protocol. Briefly, the sections of paraffin-embedded BE and BAC tissues were deparaffinized, blocked, and sequentially treated with anti-RAD51 mouse monoclonal and horseradish peroxidase- or Alexa-Fluor 488-labeled secondary antibodies, and viewed under a fluorescence microscope (Nikon, Melville, NY, USA). For western blot analyses, extracts equivalent of 50 μg protein were suspended in Laemmli’s sample buffer (0.1M Tris–HCl buffer pH 6.8, 1% sodium dodecyl sulfate, 0.05% β-mercaptoethanol, 10% glycerol and 0.001% bromophenol blue), boiled for 2 min, and electrophoresed on 4–20% glycerol gradient sodium dodecyl sulfate–polyacrylamide gel for 4 h at 120 V. Gels were electroblotted onto Trans-Blot nitrocellulose membrane (Bio-Rad Laboratories, Hercules, CA, USA) at 40V for 3 h in a Tris-glycine buffer system.
Membranes were incubated with the indicated antibodies, with constant rocking for 2 h at room temperature in phosphate-buffered saline-Tween 20 containing 1% bovine serum albumin. Blots were washed with phosphate-buffered saline-Tween 20 and incubated in either anti-rabbit or antimouse antibody conjugated to horseradish peroxidase for 2 h in phosphate-buffered saline-Tween 20 containing 3% nonfat dry milk. After washing, specific proteins were detected using an enhanced chemiluminescence detection kit, according to the instructions provided by the manufacturer (Amersham Life Sciences Inc., Arlington Heights, IL, USA).
Membranes were incubated with the indicated antibodies, with constant rocking for 2 h at room temperature in phosphate-buffered saline-Tween 20 containing 1% bovine serum albumin. Blots were washed with phosphate-buffered saline-Tween 20 and incubated in either anti-rabbit or antimouse antibody conjugated to horseradish peroxidase for 2 h in phosphate-buffered saline-Tween 20 containing 3% nonfat dry milk. After washing, specific proteins were detected using an enhanced chemiluminescence detection kit, according to the instructions provided by the manufacturer (Amersham Life Sciences Inc., Arlington Heights, IL, USA).
2-Mercaptoethanol
alexa fluor 488
Antibodies
Bromphenol Blue
Chemiluminescence
dodecyl sulfate
Esophagus
Ethics Committees, Research
Gels
Glycerin
Glycine
Homo sapiens
Horseradish Peroxidase
Immunoglobulins
Laemmli buffer
Malignant Neoplasms
Microscopy, Fluorescence
Milk, Cow's
Mus
Nitrocellulose
Paraffin Embedding
Phosphates
polyacrylamide gels
Proteins
Rabbits
Saline Solution
Serum Albumin, Bovine
Sodium-20
Sulfate, Sodium Dodecyl
Tissue, Membrane
Tissues
Tromethamine
Tween 20
Western Blot
Most recents protocols related to «Sodium-20»
Example 7
A composition comprising 5% Benzoyl peroxide (BPO) as active ingredient:
The process for the preparation of the compositions listed above was as follows:
-
- 1. Disodium EDTA and Carbomer were added to the water and homogenized;
- 2. Glycerin was added to stage 1 and the mixture was stirred;
- 3. PED-40 hydrogenated castor oil was heated to 40° C. separately and after clear liquid was obtained, it was added to stage 2;
- 4. 20% solution of sodium hydroxide was added for neutralization;
- 5. A solution of imidazolidinyl urea in water was added to stage 4;
- 6. Benzoyl peroxide was added to ethoxydiglycol separately and passed through Fryma colloid mill, twice;
- 7. Silica microspheres were added to the stage 6 and resultant mixture was stirred;
- 8. Stage 7 was added to stage 5 and the mixture was homogenized.
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carbomer
Castor oil
Colloids
EDTA, Disodium
Glycerin
hydroxide ion
imidazolidinyl urea
Microspheres
Peroxide, Benzoyl
Pharmaceutical Preparations
Silicon Dioxide
Sodium-20
Sodium Hydroxide
urea-EDTA
Example 6
The pulverized vicagrel was mixed with pregelatinized starch, microcrystalline cellulose, polyvinylpyrrolidone, and half of the amount of croscarmellose sodium and half of the amount of magnesium stearate in a V-type mixer for 10 min. The material was put into a dry granulator (LGJ-300) where granulation was operated at parameters of a feed rate of 20 Hz, roller speed of 15 rpm, extrusion force of 6 bar, screen of 20 mesh, and shearing speed of 300 rpm. The particles were mixed with the rest of the disintegration and the lubricant for 5 min to obtain drug-containing particles, which were subjected to further tableting operation.
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magnesium stearate
microcrystalline cellulose
Pharmaceutical Preparations
Povidone
Sodium, Croscarmellose
Sodium-20
Starch
vicagrel
Because both powders for injection were water-soluble, the sample solution was prepared with ultrapure water at the concentration of 200 mg mL−1 for penicillin sodium and 20 mg mL−1 for omeprazole sodium, respectively. Then the sample solution was extracted and eluted following the previously described procedure of the normal saline.
Normal Saline
Omeprazole
Penicillins
Powder
Sodium
Sodium-20
Taking 200 μl of argon-deoxygenated labeling buffer (10 mmol/L N-2-hydroxyethylpiperazine -N' -2-ethanesulfonic acid, 20 mmol/L sodium glucoheptonate with pH 6.6), adding 100 µl affibody with a concentration of 1 g/L and 0.5 μl mixtures with a concentration of 50 g/L consisting of SnCl2·2H2O and HCl, distilled water. After blending, 100 µL 99mTcO4 (about 2 mCi) was added and placed in a metal bath at 25, 37, 50, 90 and 100 °C for 4–12 min for full reaction. Use a pipette to take a reaction mixture of 0.25 μl, and spot it at 1/5 of the thin-layer chromatography paper (ITLC-SG), and use PBS and citric acid as mobile phases to perform chromatography, and use a γ counter to measure the radioactivity count, calculate yield rate. According to the above experimental steps, different reaction conditions were set up respectively to find the best experimental conditions for 99mTc labeling HER2 affibody.
Adjustment Disorders
Argon
Bath
Buffers
Chromatography
Citric Acid
erbb2 Gene
glucoheptonate
HEPES
Metals
Paper Chromatographies
Radioactivity
Sodium-20
Technetium Tc 99m Pertechnetate
Vitelliform Macular Dystrophy
To perform western blot analysis, H9c2 cells were harvested with cell lysis buffer (Mammalian Protein Extraction Reagent, 78501; Pierce Thermo Scientific, Tokyo, Japan) containing protease inhibitors (#04080-11; Nacalai Tesque Inc.) and phosphatase inhibitors (#07575-51; Nacalai Tesque Inc.) on ice for 15 min. The supernatants of protein lysates were collected after 10 min of centrifugation at 10,000 × g. The protein concentrations of cell lysates were determined using a bicinchoninic acid (BCA) protein assay kit (Thermo Fisher Scientific). The samples (5 μg) were separated on 5–20% sodium dodecyl sulfate-polyacrylamide gels (#2331830; Atto, Tokyo, Japan) and transferred onto polyvinylidene difluoride membranes (BioRad, Hercules, CA) using Trans-Blot Turbo (BioRad). After being blocked with Blocking One (#03953-95; Nacalai Tesque Inc.) for 30 min at room temperature, the membranes were washed in Tris-buffered saline containing 0.1% Tween 20 (polyoxyethylene sorbitan monolaurate, 35624-15; Nacalai Tesque Inc.) three times for 10 min and incubated with primary antibodies at 4°C overnight. The following antibodies were used as primary antibodies: monoclonal anti-rat FGF23 antibody (1:500, MAB2629; R&D Systems); polyclonal anti-goat FGF23 antibody (1:1000, ab123502; Abcam, Cambridge, UK); polyclonal anti-rabbit FGFR4 antibody (1:1000, ab119378; Abcam); polyclonal anti-rabbit FGFR4 (phospho Y642; pFGFR4) antibody (1:1000, ab192589; Abcam); polyclonal anti-rabbit furin antibody (1:1000, PA1-062; Thermo Fisher Scientific); polyclonal anti-rabbit hypoxia-inducible factor 1 alpha (HIF1α) antibody (1:1000, NB100-134; Novus Biologicals, Centennial, CO); polyclonal anti-rabbit polypeptide GALNT3 antibody (1:1000, SAB2106736; Sigma-Aldrich); and anti-rabbit α/β tubulin (1:1000, CST#2148; Cell Signaling Technology, Danvers, MA). After being washed in Tris-buffered saline containing 0.1% Tween 20 three times, the membranes were incubated with the following horseradish peroxidase-conjugated secondary antibodies: donkey anti-rabbit IgG antibody (1:5000, NA934; GE Healthcare, Bucks, UK) and goat anti-rat IgG antibody (1:10,000, NA935; GE Healthcare) for 1 h. The bands were detected by the enhanced chemiluminescent method (ECL prime; GE Healthcare or Chemi-Lumi One Ultra; Nacalai Tesque Inc.), captured using a chemiluminescence imaging system (AE-9300 Ez-capture MG; Atto), and analyzed with ImageJ Software (National Institutes of Health, Bethesda, MD).
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anti-IgG
Antibodies
Antibodies, Anti-Idiotypic
bicinchoninic acid
Biological Assay
Biological Factors
Buffers
Centrifugation
Chemiluminescence
dodecyl sulfate
Equus asinus
FGF23 protein, human
FGFR4 protein, human
Furin
Goat
HIF1A protein, human
Horseradish Peroxidase
Immunoglobulins
inhibitors
Mammals
Novus
Phosphoric Monoester Hydrolases
polyacrylamide gels
Polypeptides
Polysorbates
polyvinylidene fluoride
Protease Inhibitors
Proteins
Rabbits
Saline Solution
Sodium-20
Tissue, Membrane
Tubulin
Tween 20
Western Blot
Top products related to «Sodium-20»
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Resazurin sodium salt is a chemical compound commonly used as an indicator in various laboratory applications. It is a redox-sensitive dye that changes color based on the oxidation-reduction state of the surrounding environment. When used in cell culture systems, resazurin can be employed as a viability and cytotoxicity assay to measure cellular metabolic activity.
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The Folin-Ciocalteu reagent is a colorimetric reagent used for the quantitative determination of phenolic compounds. It is a mixture of phosphomolybdic and phosphotungstic acid complexes that undergo a color change when reduced by phenolic compounds.
Sourced in Japan, China
ExTaq HS polymerase is a high-speed and high-fidelity DNA polymerase developed by Takara Bio. It is designed for efficient and accurate DNA amplification in various molecular biology applications.
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Nitrocellulose membranes are a type of laboratory equipment designed for use in protein detection and analysis techniques. These membranes serve as a support matrix for the immobilization of proteins, enabling various downstream applications such as Western blotting, dot blotting, and immunodetection.
Sourced in United States, Germany, China
The Genesys 10S UV-Vis is a compact, single-beam ultraviolet-visible spectrophotometer. It is designed to measure the absorbance or transmittance of samples across the ultraviolet and visible light spectrum.
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Gallic acid is a naturally occurring organic compound that can be used as a laboratory reagent. It is a white to light tan crystalline solid with the chemical formula C6H2(OH)3COOH. Gallic acid is commonly used in various analytical and research applications.
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Protease is a class of enzymes that catalyze the breakdown of proteins into smaller polypeptides or amino acids. It is a fundamental tool used in various laboratory applications, such as protein purification, tissue dissociation, and sample preparation for analysis.
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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.
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The BCA Protein Assay Kit is a colorimetric detection and quantification method for total protein concentration. It utilizes bicinchoninic acid (BCA) for the colorimetric detection and quantification of total protein. The assay is based on the reduction of Cu2+ to Cu1+ by protein in an alkaline medium, with the chelation of BCA with the Cu1+ ion resulting in a purple-colored reaction product that exhibits a strong absorbance at 562 nm, which is proportional to the amount of protein present in the sample.
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Whatman No. 1 filter paper is a general-purpose cellulose-based filter paper used for a variety of laboratory filtration applications. It is designed to provide reliable and consistent filtration performance.
More about "Sodium-20"
Sodium-20 is a radioactive isotope of sodium with a half-life of approximately 17.8 seconds.
It has various research applications, including medical imaging, tracer studies, and nuclear physics experiments.
PubCompare.ai's intelligent tool can help optimize your Sodium-20 research by locating the best protocols from literature, pre-prints, and patents, enhancing reproducibility and finding the optimal solution for your experiments.
Sodium-20 is a valuable tool in the field of nuclear medicine, where it can be used as a radiotracer for medical imaging techniques like positron emission tomography (PET) and single-photon emission computed tomography (SPECT).
Its short half-life makes it suitable for time-sensitive studies, as the radioactive signal decays quickly, reducing the radiation exposure to research subjects or patients.
In addition to medical imaging, Sodium-20 is also utilized in tracer studies, where it can be used to track the movement and distribution of sodium in biological systems.
This information can be valuable for understanding various physiological processes, such as ion transport and cellular metabolism.
Furthermore, Sodium-20 has applications in nuclear physics experiments, where it can be used as a source of high-energy particles for studying nuclear reactions and the properties of atomic nuclei.
To enhance your Sodium-20 research, PubCompare.ai's advanced AI-powered tool can help you locate the best protocols from the literature, pre-prints, and patents.
This can improve the reproducibility of your experiments and help you find the optimal solution for your specific research needs.
PubCompare.ai's intelligent tool can also be useful for researchers working with other related substances, such as Resazurin sodium salt, Folin-Ciocalteu reagent, ExTaq HS polymerase, Nitrocellulose membranes, Genesys 10S UV-Vis, Gallic acid, Protease, FBS, BCA protein assay kit, and Whatman No. 1 filter paper.
By comparing protocols and finding the best practices, you can streamline your research and achieve enhanced outcomes.
Experiance enhanced research outcomes today with PubCompare.ai's advanced AI capabilities and discover the power of optimized Sodium-20 research.
It has various research applications, including medical imaging, tracer studies, and nuclear physics experiments.
PubCompare.ai's intelligent tool can help optimize your Sodium-20 research by locating the best protocols from literature, pre-prints, and patents, enhancing reproducibility and finding the optimal solution for your experiments.
Sodium-20 is a valuable tool in the field of nuclear medicine, where it can be used as a radiotracer for medical imaging techniques like positron emission tomography (PET) and single-photon emission computed tomography (SPECT).
Its short half-life makes it suitable for time-sensitive studies, as the radioactive signal decays quickly, reducing the radiation exposure to research subjects or patients.
In addition to medical imaging, Sodium-20 is also utilized in tracer studies, where it can be used to track the movement and distribution of sodium in biological systems.
This information can be valuable for understanding various physiological processes, such as ion transport and cellular metabolism.
Furthermore, Sodium-20 has applications in nuclear physics experiments, where it can be used as a source of high-energy particles for studying nuclear reactions and the properties of atomic nuclei.
To enhance your Sodium-20 research, PubCompare.ai's advanced AI-powered tool can help you locate the best protocols from the literature, pre-prints, and patents.
This can improve the reproducibility of your experiments and help you find the optimal solution for your specific research needs.
PubCompare.ai's intelligent tool can also be useful for researchers working with other related substances, such as Resazurin sodium salt, Folin-Ciocalteu reagent, ExTaq HS polymerase, Nitrocellulose membranes, Genesys 10S UV-Vis, Gallic acid, Protease, FBS, BCA protein assay kit, and Whatman No. 1 filter paper.
By comparing protocols and finding the best practices, you can streamline your research and achieve enhanced outcomes.
Experiance enhanced research outcomes today with PubCompare.ai's advanced AI capabilities and discover the power of optimized Sodium-20 research.