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Cysteamine

Cysteamine is a naturally occurring aminothiol compound that plays a crucial role in cellular metabolism.
It is involved in the catabolism of the amino acid cysteine and has been studied for its potential therapeutic applications in various medical conditions.
Cysteamine has been investigated for its ability to treat cystinosis, a rare genetic disorder characterized by the accumulation of cystine crystals in various organs.
Additionally, research suggests that cysteamine may possess neuroprotective properties and could be beneficial in the management of neurodegenerative diseases.
The versatility of cysteamine has also prompted investigations into its use as an antioxidant and its potential to modulate inflammatory processes.
Ongoing research continues to elucidate the multifaceted physiological and pharmacological aspects of this important biomoleucle.

Most cited protocols related to «Cysteamine»

1
Super-resolution Imaging of Fixed Cells
BS-C-1 cells (ATCC) were fixed, immunostained with rabbit anti-Tom20 (Santa Cruz Biotech) and/or mouse anti-β-tubulin (TUB2.1, Cytoskeleton) (See Supplementary Methods online for the detailed immunostaining procedure). The stained cells were imaged in PBS with the addition of 100 mM mercaptoethylamine at pH 8.5, 5% glucose (w/v) and oxygen scavenging enzymes (0.5 mg/mL glucose oxidase (Sigma-Aldrich), and 40 μg/mL catalase (Roche Applied Science)), unless otherwise mentioned. This above imaging buffer has a refractive index of 1.34. Media with higher refractive index (1.45) based on 80% (v/v) glycerol and 5% (w/v) glucose, or 60% (w/w) sucrose solution and 5% (w/w) glucose, were used in some experiments, both with the same amount of mercaptoethylamine and oxygen scavenging enzymes as described above. The slight mismatch between the medium refractive index and coverglass is needed for focus locking during imaging. Although a high concentration of mercaptoethylamine and oxygen scavenging system were used here for fixed cell imaging, the cyanine dyes also switch in buffers with lower concentrations of thiol and oxygen scavenger system compatible with live cell imaging12 (link).
Data acquisition was performed on a fluorescence microscope as described in the Supplementary Methods online. Specifically for 3D imaging, a cylindrical lens with a focal length of 1 m was inserted into the imaging optical path for 3D localization8 (link). To stabilize the microscope focusing during data acquisition, the reflected excitation laser from the coverglass-medium interface was directed to a quadrant photodiode. The position read out of the quadrant photodiode, which was sensitive to the distance between the coverglass and the objective focal plane, was used to provide feedback to a piezo objective positioner (Nano-F100, MadCity Labs), allowing compensation for the focus drift. The residual drift, < 40 nm (Supplementary Fig. 7 online), was corrected during data analysis. For whole cell imaging in an aqueous medium, the objective positioner was stepped in 300 nm intervals, which corresponds to a focal plane displacement of 216 nm after correcting for the refractive index mismatch at the glass-medium interface. Molecules within 270 nm below the focal plane were accepted for image reconstruction. Whole cell images were obtained from 9 partially overlapped z-slices. For imaging in media with a refractive index of 1.45, the positioner was stepped in 650 nm intervals, corresponding to an actual focal plane displacement of 580 nm. Molecules within 360 nm above and below the focal plane are accepted and whole cell images were obtained from 4 partially overlapped z-slices.
For single color imaging, the A405-Cy5 labeled sample was continuously illuminated with a 657 nm imaging laser (~30 mW). A low intensity 405 nm laser was used to activate the probes, with intensity adjusted such that only an optically resolved subset of the probes were activated at any given time. In certain cases, the 405 nm laser can be omitted because the 657 nm laser can also activate Cy5, albeit at a low rate. Emission from the fluorophores were recorded by the camera at a frame rate of 20 Hz. 3D localization of individual molecules was performed as described previously8 (link) and described in the Supplementary Methods online. Multicolor imaging was performed by illuminating the sample repetitively with each frame of an activation laser followed by 3 frames of the 657 nm imaging laser. An alternating sequence of two activation lasers was used for two-color imaging. The 405 nm, 460 nm and 532 nm lasers were used to activated A405-Cy5, A488-Cy5, and A555-Cy5, respectively. Subtraction of crosstalk between different color channels were performed during data analysis as described in the Supplementary Methods online.
Huang B., Jones S.A., Brandenburg B, & Zhuang X. (2008). Whole cell 3D STORM reveals interactions between cellular structures with nanometer-scale resolution. Nature methods, 5(12), 1047-1052.
Publication 2008
A-A-1 antibiotic Buffers Catalase Cells Cross Reactions Cysteamine Cytoskeleton Dyes Enzymes Gas Scavengers Glucose Glycerin Lens, Crystalline Microscopy Microscopy, Fluorescence Mus Oxidase, Glucose Oxygen Rabbits Reading Frames Sucrose Sulfhydryl Compounds Tubulin
2
Super-resolution Imaging of Live and Fixed Cells
Super-resolution imaging experiments were performed on live samples (Fig. 2j, Supplementary Fig. 2c, Supplementary Fig. 4d, Supplementary Fig. 4g) and fixed cells (Fig. 1i, Fig. 2b, Supplementary Fig. 2a, Supplementary Fig. 4a). For live-cell dSTORM imaging the cells were labeled, washed, and imaged directly in DMEM–FBS. For fixed cell preparations, cells were labeled, washed, and fixed in 4% paraformaldehyde (Electron Microscopy Sciences) in PBS buffer (pH = 7.5). The cells were imaged in a sealed cell chamber (Life Technologies) containing nitrogen-degassed redox buffer consisting of PBS supplemented with 50 mM mercaptoethylamine (Sigma–Aldrich), 10% w/v glucose, 0.5 mg/mL glucose oxidase (Sigma–Aldrich), and 28400 U/mL catalase (Sigma–Aldrich). Before imaging, JF549 could be efficiently “shelved” in a dark state upon illumination with 2 kW·cm−2 of excitation light (561 nm), and then activated back to a fluorescent state by blue light (405 nm) with low intensity (~20·W cm−2). JF646 fluorophores were converted into a predominately dark state using continuous illumination of 637 nm excitation light at 14 kW·cm−2, after which individual rapidly blinking molecules of JF646 fluorophores were observed. These experiments were conducted on the two wide-field microscope systems described above: the Nikon Eclipse Ti epifluorescence microscope (Fig. 1i, Fig. 2j, Supplementary Fig. 2a, Supplementary Fig. 2c, Supplementary Fig. 4g), and the custom-built three-camera microscope with an ASI RAMM frame (Fig. 2b, Supplementary Fig. 4a, Supplementary Fig. 4d).
Grimm J.B., English B.P., Chen J., Slaughter J.P., Zhang Z., Revyakin A., Patel R., Macklin J.J., Normanno D., Singer R.H., Lionnet T, & Lavis L.D. (2015). A general method to improve fluorophores for live-cell and single-molecule microscopy. Nature methods, 12(3), 244-250.
Publication 2014
Buffers Catalase Cells Cysteamine Electron Microscopy Glucose Light Microscopy Nitrogen Oxidase, Glucose Oxidation-Reduction paraform Reading Frames
3
Super-resolution Imaging of Live and Fixed Cells
Super-resolution imaging experiments were performed on live samples (Fig. 2j, Supplementary Fig. 2c, Supplementary Fig. 4d, Supplementary Fig. 4g) and fixed cells (Fig. 1i, Fig. 2b, Supplementary Fig. 2a, Supplementary Fig. 4a). For live-cell dSTORM imaging the cells were labeled, washed, and imaged directly in DMEM–FBS. For fixed cell preparations, cells were labeled, washed, and fixed in 4% paraformaldehyde (Electron Microscopy Sciences) in PBS buffer (pH = 7.5). The cells were imaged in a sealed cell chamber (Life Technologies) containing nitrogen-degassed redox buffer consisting of PBS supplemented with 50 mM mercaptoethylamine (Sigma–Aldrich), 10% w/v glucose, 0.5 mg/mL glucose oxidase (Sigma–Aldrich), and 28400 U/mL catalase (Sigma–Aldrich). Before imaging, JF549 could be efficiently “shelved” in a dark state upon illumination with 2 kW·cm−2 of excitation light (561 nm), and then activated back to a fluorescent state by blue light (405 nm) with low intensity (~20·W cm−2). JF646 fluorophores were converted into a predominately dark state using continuous illumination of 637 nm excitation light at 14 kW·cm−2, after which individual rapidly blinking molecules of JF646 fluorophores were observed. These experiments were conducted on the two wide-field microscope systems described above: the Nikon Eclipse Ti epifluorescence microscope (Fig. 1i, Fig. 2j, Supplementary Fig. 2a, Supplementary Fig. 2c, Supplementary Fig. 4g), and the custom-built three-camera microscope with an ASI RAMM frame (Fig. 2b, Supplementary Fig. 4a, Supplementary Fig. 4d).
Grimm J.B., English B.P., Chen J., Slaughter J.P., Zhang Z., Revyakin A., Patel R., Macklin J.J., Normanno D., Singer R.H., Lionnet T, & Lavis L.D. (2015). A general method to improve fluorophores for live-cell and single-molecule microscopy. Nature methods, 12(3), 244-250.
Publication 2014
Buffers Catalase Cells Cysteamine Electron Microscopy Glucose Light Microscopy Nitrogen Oxidase, Glucose Oxidation-Reduction paraform Reading Frames
4
Super-Resolution Imaging of Biological Samples

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Publication 2010
Buffers Catalase Cysteamine Fluorescence Gas Scavengers Glucose Light Microscopy Nails Oxidase, Glucose Oxygen Reading Frames Tissues
5
Evaluating China's Clean Air Actions
In this work, we built an integrated analysis framework (SI Appendix, Fig. S18) to evaluate the air quality improvements and health benefits of clean air actions in China (i.e., the 6 measures listed in Fig. 1) from 2013 to 2017. We first used the WRF-CMAQ model (20 , 21 ) to simulate the variations in PM2.5 concentrations from 2013 to 2017, during which period contributions from anthropogenic and meteorological factors were separated through scenario analysis. We then estimated the accumulated benefits of the 5-y implementation of each major control measure in 2017. Measure-specific emission abatements were quantified by applying the MEIC model (18 ) with data collected from the Ministry of Ecology and Environment of China (SI Appendix, Table S6) as inputs (19 ). Reductions in PM2.5 concentrations introduced by each measure were then evaluated using the WRF-CMAQ model, and the number of PM2.5-attributable excess deaths avoided by each measure was further quantified using the newly developed GEMM (4 (link)).
As shown in SI Appendix, Table S1, the WRF-CMAQ modeling system was utilized to simulate PM2.5 concentrations in 4 groups of scenarios. The BASE scenario group provided baseline simulations from 2013 to 2017, from which variations in PM2.5 concentrations could be derived. With additional information provided by the FixEmis scenarios (scenarios with fixed 2017 emissions and varying meteorological conditions from 2013 to 2017), the contributions of interannual meteorological variations and anthropogenic emission abatements to the 2013–2017 PM2.5 variations were separated. The air quality improvements in 2017 introduced by each measure were further derived based on the MEAS scenario and the NoCtrl scenario groups. Details of the methods and datasets are described in the SI Appendix. To evaluate CMAQ model performance, we compared simulated meteorological parameters, total PM2.5 concentrations, and PM2.5 chemical composition concentrations with ground observations (SI Appendix, sections S3 and S4).
Zhang Q., Zheng Y., Tong D., Shao M., Wang S., Zhang Y., Xu X., Wang J., He H., Liu W., Ding Y., Lei Y., Li J., Wang Z., Zhang X., Wang Y., Cheng J., Liu Y., Shi Q., Yan L., Geng G., Hong C., Li M., Liu F., Zheng B., Cao J., Ding A., Gao J., Fu Q., Huo J., Liu B., Liu Z., Yang F., He K, & Hao J. (2019). Drivers of improved PM2.5 air quality in China from 2013 to 2017. Proceedings of the National Academy of Sciences of the United States of America, 116(49), 24463-24469.
Publication 2019
Biological Models chemical composition Cysteamine Meteorological Factors

Most recents protocols related to «Cysteamine»

1
Permeability Assay for Keratinocyte and RHE Cultures
For the permeability assay of keratinocyte monolayers, we used an in vitro vascular permeability assay kit (Sigma-Aldrich). The N/TERT were plated on the 18 mm coverslips prepared according to the manufacturer’s protocol and the experimental treatment was performed as described above. Then, the samples were treated with Fluorescein-Streptavidin for 5 min and fixed with 4% paraformaldehyde for 15 min, washed in PBS 3 times, mounted on slides and imaged with the confocal microscope. The areas inside large keratinocyte islands were chosen for the imaging.
To test the basal-to-apical permeability of RHE cultures, we adapted a method used in.104 (link) The RHEs were cultured and stimulated as described above. After 24 h of stimulation, the biotin stock solution (10 mg/mL in water, Tocris, Cat.# 7302) was added directly to the media at the bottom of the inserts to the final concentration of 0.5 mg/mL. The cultures were incubated for 1 h. Then RHEs were fixed in 4% formaldehyde overnight and embedded in paraffin. 5 μm sections were cut, deparaffinized and directly stained with Fluorescein-Streptavidin (Sigma-Aldrich, Cat.# 17–10398) at 1:2000 30 min in PBS.
For the apical-to-basal permeability assay on RHE cultures, RHE cultures were moved from deep well plates to standard 12 well plates after 11 days of airlift (10 days of standard airlifted culture followed by 24 h of stimulation). In 12 well plate, 1.850 mL medium with continuous respective stimulation was added to the bottom well and 0.6 mL medium with continuous respective stimulation and 0.2 mM Na-Fluorescein (Sigma-Aldrich) was placed in the upper chamber, on top of the cornified layer. The fluorescence intensity in the bottom well was measured after 24 h of incubation with fluorescein (meas. filter 492 nm, ref. filter 570 nm).
Shutova M.S., Borowczyk J., Russo B., Sellami S., Drukala J., Wolnicki M., Brembilla N.C., Kaya G., Ivanov A.I, & Boehncke W.H. (2023). Inflammation modulates intercellular adhesion and mechanotransduction in human epidermis via ROCK2. iScience, 26(3), 106195.
Full text: Click here
Publication 2023
Biological Assay Biotin Cysteamine Fluorescein Fluorescence Formaldehyde Keratinocyte Microscopy, Confocal Paraffin Embedding paraform Permeability Streptavidin TERT protein, human Therapies, Investigational Vascular Permeability
2
Physicochemical Properties of Biomass Hydrochars
The physicochemical properties
of the raw biomass and hydrochars obtained under RSM- and GA-optimized
conditions were measured and compared. The proximate analysis, which
measures the sample’s inherent moisture, ash content, and volatile
matter, with the fixed carbon determined by the difference, was carried
out in accordance with the ASTM D-5142 standard. The CV was measured
for the samples using a Leco AC500 bomb calorimeter in accordance
with the ASTM D5865-04 standard. The ultimate and sulfur analyses
of all the samples were performed according to ASTM D 5373-02 and
ASTM D 4239-05 for CHN and total sulfur content, respectively, using
a Leco CHN 628 with an add-on 628 S module.
The raw biomass
and the optimized hydrochars were converted to ash following the CEN/TS
14588 standard, with inductively coupled plasma atomic emission spectroscopy
(ICP-AES) used to characterize the ash for heavy metals. The combustion
and co-combustion tests were conducted under an oxidizing atmosphere
using air. Approximately 100 mg of each sample was subjected to a
heating rate of 10 °C/min from room temperature to 850 °C
and held until there was a constancy in weight loss. Individual DTG
curves obtained from the combustion of the samples were used to evaluate
the sample’s combustion properties, including the initiation
of volatile matter, ITFC, peak temperature, and BT. The
BET surface area and pore volume were determined using an Autosorb
iQ-C automated gas sorption analyzer. The surface morphology was determined
and elemental analysis was performed using a Carl Zeiss Sigma Field
Emission Scanning Electron Microscope equipped with an Oxford X-act
EDS detector and transmission electron microscope FEI—Quanta
250. The functional groups were determined using a Perkin Elmer FTIR
Spectrometer—Spectrum Two over the wavenumber range of 400–4000
cm–1. The X-ray powder diffraction analysis was
conducted using a D2 PHASER Bruker Meas Srv D2-208365 with SSD 160
operated at 30 kV and 10 mA.
The MY of the hydrochars was calculated
using the following equations where MY is the mass yield, MHC is the mass of the hydrochar, and MB is the mass of the biomass sample.
Abdulsalam J., Setsepu R.L., Lawal A.I., Onifade M, & Bada S.O. (2023). Recycling of Trees Planted for Phytostabilization to Solid Fuel: Parametric Optimization Using the Response Surface Methodology and Genetic Algorithm. ACS Omega, 8(8), 7448-7458.
Publication 2023
ARID1A protein, human Carbon Cysteamine Inductively Coupled Plasma Atomic Emission Spectroscopy Metals, Heavy Powder Scanning Electron Microscopy Sulfur Transmission Electron Microscopy X-Ray Diffraction
3
Bovine Oocyte In Vitro Maturation Protocol
For in vitro maturation (IVM), bovine ovaries, collected from a local slaughterhouse, were kept in normal saline and transported to the laboratory within 2 h. Once in the laboratory, ovaries were thoroughly washed with 70% ethanol and PBS solution to avoid contamination. Subsequently, cumulus-oocyte complexes (COCs) with a diameter of about 100–130 μm and a central oocyte surrounded by at least three layers of cumulus cells were collected according to the department's protocols (32 (link)).
After collection, COCs were transferred to 500 μl of IVM droplets (40–50 COCs per droplet) covered by mineral oil and cultured for a subsequent 24 h in a CO2 incubator (38.5°C and 5% CO2). IVM medium applied in this study was TCM-199 medium supplemented with 0.3 mM sodium pyruvate, 1 μg/ml β-2-oestradiol, 2 mM GlutaMAX, 10 ng/ml EGF, 10% fetal bovine serum, 10 U/ml FSH, 10 U/ml LH and 100 μM cysteamine (67 (link)–69 (link)).
Li S., Ren J., Zhang W., Wang B., Ma Y., Su L., Dai Y, & Liu G. (2023). Glutathione and selenium nanoparticles have a synergistic protective effect during cryopreservation of bull semen. Frontiers in Veterinary Science, 10, 1093274.
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Publication 2023
Bos taurus Cumulus Cells Cysteamine Estradiol Ethanol Fetal Bovine Serum Normal Saline Oil, Mineral Oocytes Ovary Pyruvate Sodium
4
Fabrication of SU-8-Based Microelectrode Arrays
The surface MEA chip and flexible MEAs were fabricated following previous procedures with small modifications [34 (link)]. A Si wafer with a 1µm thick SiO2 layer (University Wafer Inc., South Boston, MA, USA) was first cleaned by sonicating in acetone, isopropanol, and DI water sequentially for 5 min each step. The wafer was then dried on a hot plate at 150 °C for 3 min, then the surface was cleaned and activated by O2 plasma using a reactive ion etcher (RIE, Trion Phantom III LT, Clearwater, FL, USA) for 120 s at 200 mTorr pressure and 150 Watts power. The wafer was then spin-coated with SU-8 2015 (MicroChemicals, Ulm, Germany) at 5000 rpm for 1 min and soft baked at 65 °C for 3 min and 95 °C for 5 min to evaporate solvent, then the wafer was exposed using a maskless aligner (MLA, MLA100, Heidelberg Instruments, Heidelberg, Germany) with a dose of 400 mJ/cm2. After exposure, the SU-8 first layer was post-baked at 65 °C for 3 min and 95 °C for 5 min, developed using SU-8 developer (MicroChemicals, Germany) for 1 min, and cleaned by isopropanol and DI water, Then, the wafer was hard baked at 200 °C, 180 °C, and 150 °C for 5 min each for SU-8 curing and allowed to cool down below 95 °C (step skipped for in vitro MEA fabrication). The wafer was then treated with O2 plasma to clean, activate, and roughen the SU-8 with RIE for 75 s at a pressure of 200 mTorr and 150 W power. The treated wafer was then spin-coated with AZ P4620 photoresist (MicroChemicals, Germany) at 5000 rpm for 1 min and baked at 105 °C for 5 min for resist curing. After baking, the wafer was exposed using MLA with a dose of 700 mJ/cm2, then developed using AZ400k 1:4 developer (MicroChemicals, Germany), cleaned by water rinse, and dried with N2 gas flow. A mild 120 s RIE O2 plasma treatment at pressure 600 mTorr and 60 W power was performed to clean the SU-8 before metal deposition. A 10 nm Ti adhesion layer and 100 nm Au layer were evaporated on the wafer using an Electron Beam Evaporator Plassys MEB550S (Marolles-en-Hurepoix, France). The metal was then lifted off in acetone overnight. The next day, the wafer was first rinsed with water, dried under N2 flow, and cleaned by O2 plasma for 60 s at 600 mTorr and 60 W, then spin-coated with SU-8 2015 for insulation layer at 5000 rpm for 1 min and soft baked at 65 °C for 2 min and 95 °C for 5 min. The wafer was then exposed using MLA with a dose of 400 mJ/cm2, post-backed, and developed with an SU-8 developer. The wafer was then cleaned with isopropanol and water, and was hard baked at 200 °C, 180 °C, and 150 °C for 5 min each to fully cure SU-8 and allowed to cool down below 95 °C. For in vitro use, the wafer was then cut into rectangular pieces (1.5 × 2 cm) containing an MEA and used for in vitro experiments. For in vivo use, the flexible MEAs were released from the wafer using buffered oxide etchant (1:7) (MicroChemicals, Germany) in an acid hood for 8 h to etch away the SiO2 layer. Customized PCBs were mounted with ZIF and Omnetics connectors. ZIF connectors were used to interface with flexible MEAs, and Omnetics connectors were used to interface with the potentiostat and electrophysiology recording system.
Wu B., Castagnola E, & Cui X.T. (2023). Zwitterionic Polymer Coated and Aptamer Functionalized Flexible Micro-Electrode Arrays for In Vivo Cocaine Sensing and Electrophysiology. Micromachines, 14(2), 323.
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Publication 2023
1-naphthol-8-amino-3,6-disulfonic acid Acetone Cysteamine DNA Chips Electrons Isopropyl Alcohol Metals Oxides Plasma Polychlorinated Biphenyls Pressure Solvents
5
Fabrication of Cocaine-Sensing Probes
MEA electrode sites were coated with fuzzy Au using repeated multi-step chronoamperometry (−400 mV for 1 s followed by 0 V for 1 s, 240 cycles) in a solution containing 3.5 M HAuCl4 and 0.1 M NaCl in 1.5 wt% HCl, to increase the available gold surface area. Fuzzy gold coated electrodes were immediately functionalized with cocaine-targeting aptamer using well-established protocols [37 (link)]. Next, 5 mL aliquots of 100 mM aptamer solution were incubated in 15 mL of 50 mM tris-(2-carboxyethyl) phosphine hydrochloride (TCEP, prepared in PBS) for 1 h to reduce the 5′ thiol group for gold attachment. The reduced aptamer solution was then diluted to 5 mM with PBS for electrode functionalization. Fuzzy gold coated MEAs were functionalized by soaking in aptamer solution overnight. Finally, functionalized electrodes were soaked in 30 mM 6-mercaptohexanol (MCH, prepared in PBS) or hexanethiol (HT, prepared in PBS) for 2 h to block any unreacted gold surface. The resulting cocaine sensing probes were rinsed and stored in PBS solution in the dark at 4 °C until use (Scheme 1).
Wu B., Castagnola E, & Cui X.T. (2023). Zwitterionic Polymer Coated and Aptamer Functionalized Flexible Micro-Electrode Arrays for In Vivo Cocaine Sensing and Electrophysiology. Micromachines, 14(2), 323.
Full text: Click here
Publication 2023
Cardiac Arrest Cocaine Cysteamine Gold gold tetrachloride, acid phosphine Sodium Chloride Sulfhydryl Compounds tris(2-carboxyethyl)phosphine Tromethamine

Top products related to «Cysteamine»

1
Cysteamine by Merck Group
Sourced in United States, Germany, United Kingdom, Canada, Italy
Cysteamine is a laboratory reagent used in various biochemical and analytical applications. It is a small organic molecule that serves as a reducing agent and is employed in diverse research contexts. The core function of Cysteamine is to facilitate chemical reactions and analyses where a reducing environment is required.
2
Glucose oxidase by Merck Group
Sourced in United States, Germany, Sao Tome and Principe, France, United Kingdom
Glucose oxidase is an enzyme that catalyzes the oxidation of glucose to gluconic acid and hydrogen peroxide. It is commonly used in various laboratory applications, such as the detection and measurement of glucose levels in biological samples.
3
Catalase by Merck Group
Sourced in United States, Germany, United Kingdom, Macao, Italy, Sao Tome and Principe, China, Spain, India, Australia, Canada, France, Denmark, Poland
Catalase is a common enzyme found in the cells of most living organisms. It functions as a catalyst, accelerating the decomposition of hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2).
4
N hydroxysuccinimide by Merck Group
Sourced in United States, Germany, United Kingdom, China, Italy, Canada, India, Poland, Sao Tome and Principe, France, Japan, Spain, Australia, Macao, Switzerland, Brazil, Sweden
N-hydroxysuccinimide is a chemical compound commonly used as an activating agent in organic synthesis. It is a stable, crystalline solid that can be used to facilitate the formation of amide bonds between carboxylic acids and primary amines. Its core function is to activate carboxylic acids, enabling their subsequent reaction with other functional groups.
5
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.
6
Glutaraldehyde by Merck Group
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Glutaraldehyde is a chemical compound used as a fixative and disinfectant in various laboratory applications. It serves as a cross-linking agent, primarily used to preserve biological samples for analysis.
7
Mercaptoethylamine by Merck Group
Sourced in United States
Mercaptoethylamine is a colorless, viscous liquid that is used as a reagent in various laboratory applications. It is a source of the sulfhydryl (thiol) functional group, which is commonly used in organic synthesis, biochemistry, and analytical chemistry. The core function of mercaptoethylamine is to provide a reactive thiol group that can be utilized in various chemical reactions and assays.
8
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.
9
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.
10
Phosphate buffered saline (pbs) by Merck Group
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PBS (Phosphate-Buffered Saline) is a widely used buffer solution in biological and medical research. It is a balanced salt solution that maintains a stable pH and osmotic pressure, making it suitable for a variety of applications. PBS is primarily used for washing, diluting, and suspending cells and biological samples.

More about "Cysteamine"

Cysteamine is a versatile biomolecule with a range of important functions in the body.
Also known as 2-aminoethanethiol or mercaptoethylamine, this naturally occurring aminothiol compound plays a crucial role in cellular metabolism.
It is involved in the catabolism (breakdown) of the amino acid cysteine, making it an important part of cysteine metabolism.
Research has shown that cysteamine has potential therapeutic applications in various medical conditions.
One of the primary areas of study is its use in the treatment of cystinosis, a rare genetic disorder characterized by the accumulation of cystine crystals in various organs.
By reducing cystine levels, cysteamine has been found to be an effective treatment option for this debilitating condition.
Beyond cystinosis, cysteamine has also demonstrated neuroprotective properties, suggesting it could be beneficial in the management of neurodegenerative diseases.
Its versatility extends to its potential as an antioxidant and its ability to modulate inflammatory processes.
In the laboratory, cysteamine is often used in conjunction with other compounds like glucose oxidase, catalase, N-hydroxysuccinimide, bovine serum albumin, and glutaraldehyde to facilitate various experimental protocols.
Its thiol group makes it a valuable reagent for conjugation and labeling applications.
Overall, the multifaceted nature of cysteamine continues to be an area of active research, with scientists exploring its diverse physiological and pharmacological aspects to uncover new applications and therapeutic possibilities.
By understanding the insights gained from the MeSH term description and the metadescription, researchers can optimize their protocols and enhance the reproducibility of their studies using innovative AI-driven platforms like PubCompare.ai.