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Electron Spin Resonance Spectroscopy

Electron Spin Resonance Spectroscopy (ESR) is a powerful analytical technique used to study the magnetic properties of materials containing unpaired electrons.
This non-invasive method provides insights into the structure, dynamics, and interactions of paramagnetic species, such as free radicals, transition metal ions, and defects in solids.
ESR spectrsocopy enables researchers to gain a deeper understanding of chemical and biological systems, leading to advancements in fields like materials science, biochemistry, and medicine.
By leveraging AI-driven insights, the PubCompare.ai platform helps optimize ESR protocols, enhancing reproducibility and research accuracy.
Researchers can easily locate, compare, and identify the best ESR protocols from literature, preprints, and patents, while the AI-powered analysis supports data-driven decision making to improve the quality of their esearch.

Most cited protocols related to «Electron Spin Resonance Spectroscopy»

The hph-1 mice (originally in CBA background) 19 (link) were backcrossed with C57BL6 mice for more than 10 generations and genotyped based on a protocol by Koo et al. 21 (link). Only homozygote hph-1 mice were used for experiments. Wild-type (WT) and hph-1 male mice at 24 weeks of age were infused with Ang II (0.7 mg/kg/day) using subcutaneously implanted osmotic pumps (Durect Corp.). During the 14-day infusion, blood pressure was monitored by telemetry method. Wireless blood pressure probes were implanted into the animals 10 days prior to the implantation of the osmotic pumps. The catheter of the blood pressure probe was inserted into the left carotid artery, while the body of the probe was inserted into the right flank. Animals were given 1 week to recover from the surgery. After this period, blood pressure was measured for 3 days to obtain a baseline. The osmotic pumps were then implanted on the 10th day after surgery. Measurements were made daily from 9am to 4pm at 250 Hz sampling rate. Average blood pressure was calculated daily as the average of the entire recording period. The use of animals and experimental procedures were approved by the Institutional Animal Care and Usage Committee at the University of California Los Angeles (UCLA).
Electron spin resonance determination of aortic nitric oxide and superoxide production, HPLC determination of aortic H4B content, and Western Blot determination of endothelial DHFR expression were performed as previously published 1 (link),2 (link).
Publication 2011
Animals Aorta Blood Pressure Catheters Common Carotid Artery EGLN2 protein, human Electron Spin Resonance Spectroscopy Endothelium High-Performance Liquid Chromatographies Homozygote Human Body Males Mice, House Operative Surgical Procedures Osmosis Ovum Implantation Oxide, Nitric Superoxides Telemetry Western Blotting
Seven week old male normotensive Wistar-Kyoto (WK) and spontaneously hypertensive (SHR) rats were randomly assigned either to the sedentary group (SHRsed; n=10 and WKsed; n=10) or to the exercise group (SHRex; n=10 and WKex; n=10). Exercise groups were subjected to moderate-intensity exercise on a motor-driven treadmill continuously for a period of 16 weeks. Animals were euthanized twenty-four hours after the last exercise session at the age of 23 weeks and left ventricle (LV) tissues were collected for later analyses. We performed the following experimental procedures: blood pressure measurements, echocardiographic analysis, real time RT-PCR, western blot analysis, electron paramagnetic resonance (EPR) studies, antioxidant assays, electrophoretic mobility shift assay (EMSA), reverse-phase high-performance liquid chromatography (HPLC), ELISA, and statistical analysis.
Publication 2009
Animals Antioxidants Biological Assay Chromatography, Reversed-Phase Liquid Determination, Blood Pressure Echocardiography Electron Spin Resonance Spectroscopy Electrophoretic Mobility Shift Assay Enzyme-Linked Immunosorbent Assay Left Ventricles Males Rats, Inbred SHR Rats, Inbred WKY Real-Time Polymerase Chain Reaction Tissues Western Blot

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Publication 2010
1,3-dimethylthiourea Bicarbonate, Sodium Biological Assay Buffers Capillaries Catalase Cell-Free System Cells Deferoxamine Electron Spin Resonance Spectroscopy Gas Scavengers Glucose HEPES Hydroxyl Radical Hypoxanthine Iron Metal Chelating Agents Microwaves Neurons Pentetic Acid Permeability Peroxide, Hydrogen poly(ethylene glycol)-co-poly(ethyleneimine) polyethylene glycol-superoxide dismutase Polymers Proteins Radionuclide Imaging Sodium Chloride Sulfate, Magnesium Superoxides Xanthine Oxidase
Electron Paramagnetic Resonance spectroscopy X-band (9.3 GHz) (E-Scan Bruker, Billerica, MA, USA) was used to assess ROS production and TAC. Samples were analyzed in triplicate. A 37 °C unit by Temperature and Gas Controller ‘‘Bio III’’ (Noxigen Science Transfer & Diagnostics GmbH, Elzach, Germany), interfaced with the E-Scan, was preserved. ROS production and TAC assessment methods were previously described [14 (link),23 (link),24 (link),25 (link),26 (link)].
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Publication 2020
Diagnosis Electron Spin Resonance Spectroscopy Radionuclide Imaging
SimRNA can use additional information about the RNA structure, obtained from experimental analyses, from independent computational predictions, or postulated by the user. Three types of user-specified restraints are currently implemented in SimRNA (Figure 3): on atomic positions (immobilization or flexible pinning), on inter-atomic distances (flexible tethering) and on the secondary structure (base-pairing). Positional restraints are used to restrict the movement of selected atoms, which can range from complete immobilization (frozen) to flexible pinning that keeps the atom close to its starting position. Immobilization was implemented as a modification to the sampling algorithm, while flexible pinning, and in fact all other restraints mentioned below, were implemented as additional penalty terms added to the energy function.
Distance restraints serve as pairwise flexible tethers (Supplementary Figure S7). For any pair of atoms, an allowed distance range can be specified. Departure beyond this range results in a penalty that scales linearly with the magnitude of the deviation. The allowed distance range can be based on experimental measurements of intramolecular distances, for example from the Förster Resonant Energy Transfer (FRET), or Electron Spin Resonance (ESR) experiments, or from chemical cross-linking. Further, theoretical predictions of intramolecular contacts can be utilized; e.g., from sequence covariation analysis that may identify important tertiary contacts without specifying the type of contact. This type of restraint may also be used to specify non-canonical base pairs.
The role of secondary structure restraints is to specify the desired canonical Watson–Crick (cis), and wobble base pairs; this type of restraints may include pseudoknots of any type. For specified bases that require pairing, a penalty is associated with a deviation from the reference geometries specific for a given type of contact. Secondary structure restraints are internally represented as distance restraints imposed on the atoms of the interacting bases. By default, SimRNA does not penalize the formation of base-pairs that are not specified in the file with restraints.
Publication 2015
Electron Spin Resonance Spectroscopy Energy Transfer Freezing Immobilization Movement Sequence Analysis

Most recents protocols related to «Electron Spin Resonance Spectroscopy»

Hydrodynamic diameter and zeta potential of the particles were determined by a dynamic light scattering (DLS) particle size analyzer (Malvern Nano-ZS90). Fourier transform infrared (FT-IR) spectra were measured on a FT-IR spectrometer (Vertex 80V, Bruker Germany) in the range of 4000–400 cm−1 to confirm the chemical composition and structure information. Crystal structure of Fe3O4–PLGA was analyzed using X-ray diffraction (XRD, D&ADVANCE, Bruker Germany). The morphology microstructure of the nanocomposites was observed by transmission electron microscopy (TEM) (JEM-2100F STEM, JEOL Japan) and atomic force microscope (AFM) (Multimode 8, Bruker Germany). UV-vis spectra were obtained using a PerkinElmer Lambda 35 spectrophotometer (UV-2550, SHIMADZU, Japan) to analyze the catalytic oxidation activity. The hysteresis loops (300 K) of different Fe3O4 NPs were tested on a vibrating sample magnetometer (VSM) (model 7404, LakeShore USA) to characterize their saturation magnetization. Fluorescence spectra were obtained using a fluorescence spectrum analyzer (LS55, PerkinElmer USA). Electron paramagnetic resonance (EPR) spectra were measured by JEOL JES-FA200 spectrometer (JEOL, Japan). The cytotoxicity of HeLa cell was observed by a fluorescence microplate reader (Synergy TM MX, Berton Corporation USA), and the ROS was observed on fluorescence microscope (Olympus IX71) and confocal laser scanning microscope (Leica TCS SP5 II).
Publication 2023
chemical composition Cytotoxin Electron Spin Resonance Spectroscopy enzyme activity Fluorescence HeLa Cells Hydrodynamics Microscopy, Atomic Force Microscopy, Confocal, Laser Scanning Microscopy, Fluorescence Oxide, Ferrosoferric Polylactic Acid-Polyglycolic Acid Copolymer Stem, Plant Transmission Electron Microscopy X-Ray Diffraction
Electron paramagnetic resonance (EPR) was used to measure the production of ·OH by using 50 mM of DMPO as the spin trapper.31 The samples were prepared as following: Fe3O4–PLGA (20 μg mL−1) with 10 mM H2O2 in pH 5.0 buffer, Fe3O4/GOx–PLGA (20 μg mL−1) in pH 5.0 buffer with 5 mM β-d-glucose, 10 mM H2O2 in pH 5.0 buffer for control. The spectra of DMPO/·OH were collected with an interval of 10 min.
Publication 2023
2,2-dimethyl-5-hydroxy-1-pyrrolidinyloxy Buffers Electron Spin Resonance Spectroscopy Glucose Oxide, Ferrosoferric Peroxide, Hydrogen Polylactic Acid-Polyglycolic Acid Copolymer

O2 concentration in whole blood was determined immediately after blood removal. 25 µL of whole blood were mixed with an aliquot of 25 µL freshly thawed CMH (1-Hydroxy-3-methoxycarbonyl-2,2,5,5-tetramethylpyrrolidine) spin probe solution. The CMH solution contained 400 µM CMH spin probe, 25 µM deferoxamine, and 5 µM diethyldithiocarbamate to chelate transition metal ions in Krebs-HEPES-Buffer (KHB) (Noxygen, Elzach, Germany). After mixing whole blood with CMH spin probe solution, it was transferred to a 50 µL glass capillary, sealed, and measured with an EMXnano electron spin resonance (ESR) spectrometer (Bruker, Billerica, MA, USA) after 5 min incubation at 37°C (Bio-III, Noxygen, Elzach, Germany). The device settings are detailed in the Supplements. Radical concentration was quantified by comparison with a series of CP° (3-Carboxy-2,2,5,5-tetramethyl-1-pyrrolidinyloxy) radical standards solved in KHB. As a blank sample, KHB added to the respective amount of CMH spin probe solution was measured and subtracted from the sample value.
For determination of radical production by immune cells, 25 µL of a cell suspension containing 2.5 × 106 cells/mL RPMI 1640 medium (Glucose 1.8 mg/mL, Glutamine 0.6 mg/mL, NaHCO3 100 µg/mL) were mixed with 25 µL of CMH spin probe solution. In contrast to whole blood, cell samples were measured over a 30 min interval to calculate the radical production rate. A sample of RPMI 1640 medium mixed 1:1 with CMH spin probe solution was used as a blank value for measuring cell suspensions and subtracted from sample values. Data were evaluated with the Xenon_nano software (version 1.3; Bruker BioSpin GmbH, Rheinstetten, Germany) and Microsoft Excel. Results regarding ROS determination by ESR were included in a dissertation by one of our co-authors (51 ). Additionally, the extracellular H2O2 concentration was determined in a suspension of 1 × 106 PBMCs/granulocytes in 100 µL PBS after 30 min at RT. A three-electrode setup that has been previously thoroughly described was used for this purpose (52 (link)). The determination of the H2O2 concentration was not performed for each animal due to limited availability of the measurement device.
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Publication 2023
Animals Bicarbonate, Sodium BLOOD Buffers Capillaries CASP7 protein, human Cells Deferoxamine Dietary Supplements Diethyldithiocarbamate Electron Spin Resonance Spectroscopy Glucose Glutamine Granulocyte HEPES Ions Medical Devices Peroxide, Hydrogen Transition Elements Xenon
The micromorphologies and composition were studied by field emission scanning electron microscopy (SEM, HITACHI, SU8020, Japan) and Flourier transformed infrared spectroscopy (FT-IR, 4000–400 cm−1, Nicolet 6700 apparatus, Thermo Fisher Scientific, U.S.). The ion concentration in solution was measured by ICP-AES (Optima 7300V, PerkinElmer, U.S.). Vibrating sample magnetometry was applied to measure the magnetic properties (VSM, MPMS-SQUID VSM-094, Quantum Design, U.S.). N2 adsorption–desorption analysis was performed for chitosan and MCT using a surface area and porosity analyzer (BET, ASAP 2020, Micromeritics Instrument Corp., U.S.). The enhanced photocatalytic mechanism was studied by X-ray photoelectron spectroscopy (XPS, ESCALAB 250Xi, Thermo Fisher Scientific, U.S.), ultraviolet-visible spectrometry (UV-vis, UV-752N, Shanghai Precision and Scientific Instrument Co., Ltd, China), ultraviolet-visible diffuse reflection spectroscopy (UV-DRS, ESCALAB 250Xi, Thermo Fisher Scientific, U.S.), electron paramagnetic resonance (EPR, Bruker E-500, Switzerland), time-of-flight mass Spectrometry (MS, Orbitrap Fusion™ Tribrid™, Thermo Scientific, U.S.), and liquid chromatography (HPLC, Agilent 1200, U.S.).
Publication 2023
1-methyl-1-piperidinomethane sulfonate Adsorption Chitosan Electron Spin Resonance Spectroscopy High-Performance Liquid Chromatographies Liquid Chromatography Mass Spectrometry Reflex Scanning Electron Microscopy Spectrophotometry, Ultraviolet Spectrum Analysis Squid

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Publication 2023
Diamines Electron Spin Resonance Spectroscopy Hydroxyl Radical Oxides pyrroline Quartz Singlet Oxygen

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More about "Electron Spin Resonance Spectroscopy"

Electron Paramagnetic Resonance (EPR) Spectroscopy, Paramagnetic Species, Free Radicals, Transition Metal Ions, Defects in Solids, Materials Science, Biochemistry, Medicine, EMX Spectrometer, D8 Advance, ESCALAB 250Xi, JES-FA200, A300-10/12, EMXplus, EScan, A300 Spectrometer, UV-3600, EMXplus Spectrometer