Experiments were carried out on a 3T whole-body scanner (Philips Medical Systems, Best, The Netherlands). A body coil was used for radio-frequency transmission and an 8-channel head coil for reception. Data were acquired according to our published methods28 . PRESS8 and scalar difference editing9 (link) were used for measuring 2HG in brain tumors. For editing, two 20-ms Gaussian 180° pulses, tuned to 1.9 p.p.m., were switched on and off in alternate scans to generate an edited H2 signal at 4.02 p.p.m. in difference spectra. The echo times of PRESS and editing were 97 and 106 ms, respectively. The quantum-mechanical simulations were carried out by means of the product-operator-based transformation matrix algorithm (Supplementary Methods ). For in vivo MR scans, following the survey imaging, T2w-FLAIR images were acquired to identify tumor regions. For single-voxel localized data acquisition, a 2×2×2 cm3 voxel was positioned within the tumor mass. PRESS acquisition parameters included sweep width = 2500 Hz, 2048 sampling points, repetition time = 2 s, and 64 averages (scan time 2.1 min). Editing data were acquired with 384 averages (scan time 13 min). An unsuppressed water signal was acquired with echo time = 14 ms and repetition time = 20 s for use as reference in metabolite quantification. Spectroscopic imaging data were acquired, using the optimized PRESS echo time, from a 1.5-cm thick slice with resolution of 1×1 cm2. Undersampling of k-space data by 20% was employed, the scan time being approximately10 min (2 averages; repetition time = 1.3 s). Data were zero filled for the un-acquired k-space points and filtered with a cosine function prior to Fourier transformation.
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MS 180
MS 180
MS 180 is a type of mass spectrometry technique used in bioreearch.
PubCompare.ai enhaces reproducibility and accuracy for MS 180 experiments by using AI-driven protocol optimization to help researchers identify the best protocols from literature, preprints, and patents.
The comparison tools provided by PubCompare.ai also aid in selecting the optimal products and methods, taking the guesswork out of MS 180 research.
PubCompare.ai enhaces reproducibility and accuracy for MS 180 experiments by using AI-driven protocol optimization to help researchers identify the best protocols from literature, preprints, and patents.
The comparison tools provided by PubCompare.ai also aid in selecting the optimal products and methods, taking the guesswork out of MS 180 research.
Most cited protocols related to «MS 180»
Brain Neoplasms
ECHO protocol
Head
Human Body
MS 180
Neoplasms
Pulses
Radionuclide Imaging
Spectrum Analysis
Strains
Transmission, Communicable Disease
Brain Neoplasms
ECHO protocol
Head
Human Body
MS 180
Neoplasms
Pulses
Radionuclide Imaging
Spectrum Analysis
Strains
Transmission, Communicable Disease
Nygren's model [35] of the human atrial action potential (AP) was implemented to reproduce the cellular electrical activity. In this study, the electrophysiological heterogeneity was introduced to reproduce APs in different parts of the atria [36] : CT, PM, APG, AVR and AWM (atrial working myocardium), which includes the remaining atrial structures. The maximum conductance values of It, IKr and ICaL were modified in Nygren's cellular model to obtain different AP models (see control values in Table 2 ).
The basic equation to calculate transmembrane voltage Vm is: where Cm is the specific membrane capacitance (50 pF), Iion is the total membrane ionic current, Vm is the membrane potential and Istim is the stimulus current.
To reproduce atrial electrical remodeling, changes in the maximum conductance and kinetics of different ionic channels of human atrial cells observed in experimental studies of chronic AF [7] have been incorporated into the AP models. The following parameters were altered [37] : maximum conductance of IK1 was increased by 250% while the maximum conductance values of ICaL and It were decreased by 74% and by 85%, respectively (see remodeled values inTable 2 ), the time constant of the fast inactivation of ICaL was increased by 62%, the activation curve of It was shifted by +16 mV, and the inactivation curve of INa was shifted by +1.6 mV.
Figure 3 depicts the APs for the different atrial cellular models considered, under both physiological (control) and remodeling conditions (Figure 3A and 3B , respectively). In these figures, we present the last AP obtained when a train of 10 stimuli at a basic cycle length of 1000 ms was applied. The corresponding APD90 (APD to 90% of repolarization) values for the different atrial cells (both for control and remodeling conditions) are shown in Table 2 . Under control conditions, APD90 showed high values (ranged from 180 ms to 307 ms) in agreement with experimental data [7] , [36] and a great APD dispersion was observed (APD90max – APD90min = 127 ms). By contrast, under remodeling conditions, the APD decreased (ranged from 56 ms to 92 ms) and a smaller APD dispersion was observed (APD90max – APD90min = 36 ms). Figure 3C shows the APD90 restitution curve for control and remodeled cells when the coupling interval (CI) between pulses is increased. Remodeling conditions not only induce a shortening in the APD90 but also reduce the frequency dependent adaptation of APD90.
The basic equation to calculate transmembrane voltage Vm is: where Cm is the specific membrane capacitance (50 pF), Iion is the total membrane ionic current, Vm is the membrane potential and Istim is the stimulus current.
To reproduce atrial electrical remodeling, changes in the maximum conductance and kinetics of different ionic channels of human atrial cells observed in experimental studies of chronic AF [7] have been incorporated into the AP models. The following parameters were altered [37] : maximum conductance of IK1 was increased by 250% while the maximum conductance values of ICaL and It were decreased by 74% and by 85%, respectively (see remodeled values in
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Acclimatization
Action Potentials
Cells
Electricity
Genetic Heterogeneity
Heart Atrium
Homo sapiens
Ion Channel
Ion Transport
Kinetics
Membrane Potentials
MS 180
Myocardium
physiology
Pulses
Somatostatin-Secreting Cells
Tissue, Membrane
To identify brain responses that reliably reflected both within-subject and between-subject variability in pain ratings, we first performed point-by-point statistical analyses (e.g., for each time-frequency point) and then confirmed the results using region-of-interest (ROI)-based statistical analyses, both in the time domain and the time-frequency domain. The procedures of the point-by-point statistical analyses are described in SI Appendix .
In addition, to verify the results obtained by the point-by-point analyses, we identified magnitudes of laser-elicited brain responses in the time and time-frequency domains and assessed their within-subject and between-subject relationships with pain intensity ratings. Baseline-to-peak amplitudes of N1, N2, and P2 waves were measured in the time-domain waveforms for each subject (N1 wave: C4-Fz, 120 to 200 ms; N2 wave: Cz-nose, 180 to 300 ms; P2 wave: Cz-nose, 250 to 500 ms) (38 (link)). The magnitudes of three time-frequency features (LEP, α-ERD, and γ-ERS) were measured in each subject, by computing the top 20% of all time-frequency points within their respective time-frequency regions-of-interest (TF-ROIs) (43 (link), 44 (link)), at Cz-nose: LEP (100 to 400 ms, 1 to 10 Hz), α-ERD (600 to 900 ms, 7 to 13 Hz), and γ-ERS (180 to 260 ms, 60 to 85 Hz) (23 (link), 45 (link), 46 (link)).
To explore the within-subject trial-by-trial relationship between brain responses and pain intensity ratings, we related the magnitudes of all LEP features with the corresponding ratings of pain perception intensity, using a correlation analysis for each subject. The obtained correlation coefficients were transformed to z values using the Fisher r-to-z transformation, and the z values were finally compared against zero using a one-sample t test. To explore the between-subject relationship between the brain responses and pain intensity ratings, we correlated the average magnitudes of all LEP features with pain intensity ratings across the whole population. To account for multiple comparisons over response features, the significance level (expressed as P value) was corrected using a false discovery rate procedure (47 ).
In addition, to verify the results obtained by the point-by-point analyses, we identified magnitudes of laser-elicited brain responses in the time and time-frequency domains and assessed their within-subject and between-subject relationships with pain intensity ratings. Baseline-to-peak amplitudes of N1, N2, and P2 waves were measured in the time-domain waveforms for each subject (N1 wave: C4-Fz, 120 to 200 ms; N2 wave: Cz-nose, 180 to 300 ms; P2 wave: Cz-nose, 250 to 500 ms) (38 (link)). The magnitudes of three time-frequency features (LEP, α-ERD, and γ-ERS) were measured in each subject, by computing the top 20% of all time-frequency points within their respective time-frequency regions-of-interest (TF-ROIs) (43 (link), 44 (link)), at Cz-nose: LEP (100 to 400 ms, 1 to 10 Hz), α-ERD (600 to 900 ms, 7 to 13 Hz), and γ-ERS (180 to 260 ms, 60 to 85 Hz) (23 (link), 45 (link), 46 (link)).
To explore the within-subject trial-by-trial relationship between brain responses and pain intensity ratings, we related the magnitudes of all LEP features with the corresponding ratings of pain perception intensity, using a correlation analysis for each subject. The obtained correlation coefficients were transformed to z values using the Fisher r-to-z transformation, and the z values were finally compared against zero using a one-sample t test. To explore the between-subject relationship between the brain responses and pain intensity ratings, we correlated the average magnitudes of all LEP features with pain intensity ratings across the whole population. To account for multiple comparisons over response features, the significance level (expressed as P value) was corrected using a false discovery rate procedure (47 ).
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Brain
Diencephalon
MS 180
N100 Evoked Potentials
N200 Evoked Potentials
Nose
P200 Evoked Potentials
Pain
Pain Perception
Severity, Pain
Temporal Lobe
Data were analyzed as described previously28 . Following a 1-Hz apodization, spectra were fitted with LCModel software19 (link), using calculated spectra of 20 metabolites as basis functions. The basis set included spectra of 2HG, NAA, GABA, glutamate, glycine, creatine, myo-inositol, glutamine, lactate, alanine, acetate, aspartate, ethanolamine, glutathione, phosphorylethanolamine, scyllo-inositol, taurine, N-acetylaspartylglutamate, glucose, and choline. The metabolite concentrations were estimated with respect to the short echo time water signal. Assuming an equal composition of gray and white matter in tumors, we used a water concentration value of 42.3 M, calculated from the literature values23 (link) for the water concentrations in gray and white matter. Relaxation effects on metabolite signals were corrected using published metabolite T2 and T1; T2 = 150, 230 and 280 for Cr, Cho and NAA, and 180 ms for other metabolites, respectively, and T1 = 1.2 for 2HG, glutamate, glutamine and myo-inositol, and 1.5 for other metabolites20 (link)–22 .
Acetate
Alanine
Aspartate
Choline
Creatine
ECHO protocol
Ethanolamine
gamma Aminobutyric Acid
Glucose
Glutamate
Glutamine
Glutathione
Glycine
Inositol
Lactates
MS 180
N-acetyl-aspartyl-glutamate
Neoplasms
phosphoethanolamine
scyllitol
Taurine
White Matter
Most recents protocols related to «MS 180»
LC-MS/MS analyses were performed using a nanoLC Ultra 1D plus (Eksigent Technologies, AB SCIEX, Foster City, CA) coupled to a SCIEX TripleTOF 5600 Mass Spectrometer System (RRID : SCR_018053) via a Nanospray III source. Tryptic peptides were solubilized using solvent A (2% acetonitrile [ACN] in water, 0.1% FA) and the concentration was determined using Thermo Fisher Qubit fluorimeter (RRID : SCR_018095), according to manufacturer’s instructions. Tryptic peptides (1 µg) were loaded on a C18 Acclaim PepMap™ 100 trapping column (Thermo Scientific, 100 µm I.D. × 2 cm, 5 µm particle diameter, 100 Å) using solvent A at 2 µL/min and, after desalting, switched online with an Acquity UPLC® M-Class Peptide BEH C18 analytical Column (Waters, 75 µm × 15 cm, 1.7 µm, 130 Å). Peptides were fractionated at a flow rate of 250 nL/min in a 250 min gradient with increasing concentrations of ACN (2% to 90%). TripleTOF 5600 system was operated in positive ion mode as follows: ion spray voltage 2300 V, curtain gas (CUR) 35, interface heater temperature (IHT) 150°C, ion source gas 1 (GS1) of 25, and declustering potential (DP) of 100 V. Data were acquired in information-dependent acquisition (IDA) mode with Analyst®TF 1.7 Software (SCIEX, USA; RRID : SCR_015785). IDA parameters were: survey scan in the mass range of 350–1250 m/z, accumulation time 250 ms, followed by MS2 spectrum accumulation for 100 ms (100–1800 m/z) in a cycle of 4.04 sec. MS/MS fragmentation criteria were: ions in the 350-1250 m/z range with a charge state of 2–5 and an abundance threshold greater than 90 counts. Dynamic exclusion was set to 15s. IDA rolling collision energy (CE) parameter script was used to control the CE.
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acetonitrile
Ions
MS 180
peptide M, retinal S antigen
Peptides
Radionuclide Imaging
Solvents
Tandem Mass Spectrometry
Trypsin
Z 350
A 100-day-old male zebrafish was treated with an anesthetic (MS-222) and wiped off the water. The zebrafish is then attached to the foam using medical tape and placed in a scanning room. Whole zebrafish were scanned using an Micro CT system (SkyScan 1276, Bruker, Germany). The camera type is XIMEA MH110XC-KK-TP and the pixel size is 17.420um. The voltage and current are 55kV and 200uA respectively. Each constant motion scan resulted in 4668 projections over 180° with an exposure time of 175 ms per projection. The exposure is 517 ms. Each zebrafish is imaged after two or three scans, covering the head, belly and tail. The three-dimensional (3D) images of the bones were obtained by Skyscan CTAn software (v.1.1.7, Skyscan CTAn, Kontich, Belgium). At least three adults in each genotype were scanned.
The 100-day-old zebrafish was anesthetized, the tissue was removed, and the spine, about 20-25 sections, was obtained. The spine were scanned using an Micro CT system (SkyScan 1276, Bruker, Germany). Each constant motion scan resulted in 686 projections. The parameters are consistent with Micro CT. Each spine is imaged after two scans. The Skyscan CTAn software was used to calculate the bone density of each section and the bone density of all sections of the spine was averaged. At least three adults in each genotype were scanned.
The 100-day-old zebrafish was anesthetized, the tissue was removed, and the spine, about 20-25 sections, was obtained. The spine were scanned using an Micro CT system (SkyScan 1276, Bruker, Germany). Each constant motion scan resulted in 686 projections. The parameters are consistent with Micro CT. Each spine is imaged after two scans. The Skyscan CTAn software was used to calculate the bone density of each section and the bone density of all sections of the spine was averaged. At least three adults in each genotype were scanned.
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Adult
Anesthetics
Bone Density
Bones
Genotype
Head
Males
MS-222
MS 180
Tail
Tissues
Vertebral Column
X-Ray Microtomography
Zebrafish
Peptides were separated by an Easy
nLC-1000, chromatographic instrument coupled to a Q-Exactive “Classic”
mass spectrometer (both from Thermo Scientific, Bremen, Germany).
For preliminary analysis, 1 μL of the peptide mixture was separated
using a linear gradient of 75 min at a flow rate of 230 nL/min on
a 15 cm, 75 μm i.d., in-house-made column packed with 3 μm
C18 silica particles (Dr. Maisch). The binary gradient
was performed using mobile phase A (0.1% FA, 2% ACN) and mobile phase
B (0.1% FA and 80% ACN). Peptide elution was obtained at a flow rate
of 230 nL/min and ramped from 6% B to 42% B in 60 min and from 42%
B to 100% B in an additional 8 min; the column was cleaned by running
100% B for 5 min. For preliminary analysis, the Q-Exactive mass spectrometer
operated in DDA mode using a top-12 method. The MS full scan range
was 350–1800 m/z, with a
resolution of 70 000, an ACG target of 1e6, and a maximum injection
time of 50 ms. The mass window for precursor ion isolation was 1.6 m/z, with a resolution of 35 000,
an AGC target of 1e5, a maximum injection time of 120 ms, an HCD fragmentation
at normalized collision energy of 25, and dynamic exclusion of 15
s.
For the construction of the spectral library, the 10 fractions
obtained by high-pH reversed-phase C18 fractionation were
separated using a linear gradient of 140 min at a flow rate of 230
nL/min on a 15 cm, 75 μm i.d., in-house-made column packed with
3 μm C18 silica particles. Peptide elution was obtained
using a gradient from 3% B to 25% B in 90 min, from 25% B to 40% B
in 30 min, from 40% B to 100% B in 8 min, and then at 100% B for 10
min. The mass spectrometer was acquired in DDA mode using the same
parameters described above.
Each EPS-urine sample was analyzed
in DIA mode with the same chromatographic
method used for fraction analysis with a unique shrewdness: every
10 analyses, at the end of the gradient, 100% B was maintained for
70 min instead of 10; this procedure allowed for more effective regeneration
of the column and, consequently, longer chromatographic performance.
The DIA method enclosed 26 windows with a full scan at resolution
of 17 500 (AGC target of 1e6 and maximum injection time of
50 ms) and DIA scans with 35 000 (AGC target of 5e5, maximum
injection time of 120 ms, and normalized collision energy of 25).
In detail, the total number of windows was 26, including 20 windows
with an isolation width of 20 m/z, 5 windows with an isolation width of 50 m/z, and 1 window with an isolation width of 200 m/z. The resulting m/z range was from 350 to 1200
Th.
nLC-1000, chromatographic instrument coupled to a Q-Exactive “Classic”
mass spectrometer (both from Thermo Scientific, Bremen, Germany).
For preliminary analysis, 1 μL of the peptide mixture was separated
using a linear gradient of 75 min at a flow rate of 230 nL/min on
a 15 cm, 75 μm i.d., in-house-made column packed with 3 μm
C18 silica particles (Dr. Maisch). The binary gradient
was performed using mobile phase A (0.1% FA, 2% ACN) and mobile phase
B (0.1% FA and 80% ACN). Peptide elution was obtained at a flow rate
of 230 nL/min and ramped from 6% B to 42% B in 60 min and from 42%
B to 100% B in an additional 8 min; the column was cleaned by running
100% B for 5 min. For preliminary analysis, the Q-Exactive mass spectrometer
operated in DDA mode using a top-12 method. The MS full scan range
was 350–1800 m/z, with a
resolution of 70 000, an ACG target of 1e6, and a maximum injection
time of 50 ms. The mass window for precursor ion isolation was 1.6 m/z, with a resolution of 35 000,
an AGC target of 1e5, a maximum injection time of 120 ms, an HCD fragmentation
at normalized collision energy of 25, and dynamic exclusion of 15
s.
For the construction of the spectral library, the 10 fractions
obtained by high-pH reversed-phase C18 fractionation were
separated using a linear gradient of 140 min at a flow rate of 230
nL/min on a 15 cm, 75 μm i.d., in-house-made column packed with
3 μm C18 silica particles. Peptide elution was obtained
using a gradient from 3% B to 25% B in 90 min, from 25% B to 40% B
in 30 min, from 40% B to 100% B in 8 min, and then at 100% B for 10
min. The mass spectrometer was acquired in DDA mode using the same
parameters described above.
Each EPS-urine sample was analyzed
in DIA mode with the same chromatographic
method used for fraction analysis with a unique shrewdness: every
10 analyses, at the end of the gradient, 100% B was maintained for
70 min instead of 10; this procedure allowed for more effective regeneration
of the column and, consequently, longer chromatographic performance.
The DIA method enclosed 26 windows with a full scan at resolution
of 17 500 (AGC target of 1e6 and maximum injection time of
50 ms) and DIA scans with 35 000 (AGC target of 5e5, maximum
injection time of 120 ms, and normalized collision energy of 25).
In detail, the total number of windows was 26, including 20 windows
with an isolation width of 20 m/z, 5 windows with an isolation width of 50 m/z, and 1 window with an isolation width of 200 m/z. The resulting m/z range was from 350 to 1200
Th.
cDNA Library
Chromatography
Fractionation, Chemical
isolation
M-200
MS 180
Peptides
Radionuclide Imaging
Silicon Dioxide
Urine
We performed synchrotron X-ray micro-computed tomography at the I12 beamline of the Diamond Light Source, United Kingdom [20 (link)]. The X-ray beam was set to a monochromatic energy of 90 keV (double bent Laue Si 111 monochromator). The regions of interest were scanned in I12 Experimental Hutch One using the beamline's modular imaging system. This detector consists of a PCO.edge 5.5 sCMOS camera and four user-selectable optical modules, each comprising a scintillator, 90-degree turning mirrors and a visible light lens. We used module 2 with a magnification of 0.820, corresponding to a recorded pixel size of 7.91 µm. Each acquisition consisted of 1800 projections, of 15 ms exposure time each, over a 180° rotation of the sample. Additionally, 50 flatfield images (sample out of the beam) were recorded before and after the series of acquisition as well as 10 dark images (X-ray beam off to record the noise of the camera).
The tomographs were reconstructed using the SAVU tomographic processing software [21 (link),22 ] developed at Diamond Light Source. In the reconstruction process, ring artefact removal [23 (link)] and auto-centring [24 (link)] were applied, as well as distortion correction [25 (link)]. The low-pass filter approach [26 (link)] was applied. Filtered back-projection reconstructions were performed using the Astra library [27 (link),28 (link)], and the whole process was applied on an HPC cluster system using the SAVU tomography pipeline.
The tomographs were reconstructed using the SAVU tomographic processing software [21 (link),22 ] developed at Diamond Light Source. In the reconstruction process, ring artefact removal [23 (link)] and auto-centring [24 (link)] were applied, as well as distortion correction [25 (link)]. The low-pass filter approach [26 (link)] was applied. Filtered back-projection reconstructions were performed using the Astra library [27 (link),28 (link)], and the whole process was applied on an HPC cluster system using the SAVU tomography pipeline.
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Diamond
DNA Library
Lens, Crystalline
Light
Light, Visible
MS 180
Radiography
Reconstructive Surgical Procedures
Tomography
Vision
X-Ray Microtomography
SHeM data for the glass material system was collected in a single micrograph with 1000/1500 ms dwell. An image with a suitable background region for contrast calculations was conducted with identical dwell. The diamond material system used 5 component images, each with 1200/1800 ms dwell, which were then summed to produce the final micrograph. An image with a suitable background region was conducted with 1200/9000 ms dwell. Errors in the contrast are estimated using the standard deviation of the intensity in the regions used to calculate contrast and standard error propagation.
Full text: Click here
Diamond
MS 180
Top products related to «MS 180»
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The Q Exactive mass spectrometer is a high-resolution, accurate-mass (HRAM) instrument designed for advanced proteomics, metabolomics, and small molecule applications. It combines a quadrupole mass filter with a high-field Orbitrap mass analyzer to provide precise mass measurements and high-quality data.
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MATLAB is a high-performance programming language and numerical computing environment used for scientific and engineering calculations, data analysis, and visualization. It provides a comprehensive set of tools for solving complex mathematical and computational problems.
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The Shimadzu Prominence nanoLC system is a high-performance liquid chromatography (HPLC) instrument designed for nanoscale separations. It is capable of performing sensitive analyses of samples with low analyte concentrations, such as those found in proteomics and metabolomics research. The system features a low-flow-rate pump, a high-pressure mixing system, and an autosampler, enabling precise and reproducible nanoscale separations.
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The Q Exactive™ Plus is a high-resolution, accurate-mass quadrupole-Orbitrap mass spectrometer. It is designed for sensitive and robust performance in a wide range of applications.
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The TripleTOF 5600 is a high-resolution mass spectrometer designed for advanced analytical applications. It combines a triple quadrupole front-end with a time-of-flight (TOF) mass analyzer, providing high sensitivity and accurate mass measurements. The instrument is capable of performing various modes of operation, including full-scan acquisition, targeted data-dependent acquisition, and independent data acquisition.
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The Analyst TF 1.7 is a triple quadrupole mass spectrometer designed for high-performance liquid chromatography (HPLC) and ultra-high-performance liquid chromatography (UHPLC) applications. It provides precise, sensitive, and reliable quantitative analysis of a wide range of analytes.
Sourced in United States, Canada, Japan, Germany, Australia, United Kingdom
The TripleTOF 5600 is a high-resolution mass spectrometer designed for advanced analytical applications. It features a combination of a triple quadrupole and a time-of-flight mass analyzer, providing high sensitivity and mass accuracy. The TripleTOF 5600 is capable of performing a variety of analytical techniques, including quantitative and qualitative analysis of small molecules, proteins, and other biomolecules.
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The Ekspert MicroLC 200 Plus System is a liquid chromatography instrument designed for analytical-scale separations. It features a high-pressure liquid chromatography (HPLC) pump, an autosampler, and a column oven. The system is capable of handling micro-flow rates for applications requiring small sample volumes or low solvent consumption.
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The Avance III is a high-performance NMR spectrometer by Bruker. It is designed for advanced nuclear magnetic resonance applications, providing reliable and accurate data acquisition and analysis capabilities.
More about "MS 180"
MS 180 is a type of mass spectrometry (MS) technique used extensively in bioresearch.
It is a powerful analytical tool that allows researchers to accurately identify and quantify a wide range of biomolecules, including proteins, peptides, metabolites, and lipids.
The MS 180 technique is often coupled with other advanced instruments, such as the Q Exactive mass spectrometer, MATLAB software for data analysis, and the Prominence nanoLC system for liquid chromatography separation.
Researchers conducting MS 180 experiments can face challenges in ensuring reproducibility and accuracy.
This is where PubCompare.ai comes in.
This AI-driven platform helps optimize protocols and identify the best experimental methods from literature, preprints, and patents.
By using PubCompare.ai's comparison tools, researchers can select the optimal products, instruments, and procedures for their MS 180 studies, taking the guesswork out of the process.
PubCompare.ai's features also extend to other mass spectrometry techniques, such as the Q ExactiveTM Plus, TripleTOF 5600, Analyst TF 1.7, TripleTOF 5600 mass spectrometer, and the Ekspert MicroLC 200 Plus System.
The platform's comprehensive approach to protocol optimization and product selection can benefit researchers working with a variety of mass spectrometry methods, including those using the Desktop Micro Computer Tomograph "µCT 40" and the Avance III NMR spectrometer.
By leveraging the insights and tools provided by PubCompare.ai, researchers can enhance the reproducibility and accuracy of their MS 180 experiments, leading to more reliable and impactful findings in the field of bioresearch.
It is a powerful analytical tool that allows researchers to accurately identify and quantify a wide range of biomolecules, including proteins, peptides, metabolites, and lipids.
The MS 180 technique is often coupled with other advanced instruments, such as the Q Exactive mass spectrometer, MATLAB software for data analysis, and the Prominence nanoLC system for liquid chromatography separation.
Researchers conducting MS 180 experiments can face challenges in ensuring reproducibility and accuracy.
This is where PubCompare.ai comes in.
This AI-driven platform helps optimize protocols and identify the best experimental methods from literature, preprints, and patents.
By using PubCompare.ai's comparison tools, researchers can select the optimal products, instruments, and procedures for their MS 180 studies, taking the guesswork out of the process.
PubCompare.ai's features also extend to other mass spectrometry techniques, such as the Q ExactiveTM Plus, TripleTOF 5600, Analyst TF 1.7, TripleTOF 5600 mass spectrometer, and the Ekspert MicroLC 200 Plus System.
The platform's comprehensive approach to protocol optimization and product selection can benefit researchers working with a variety of mass spectrometry methods, including those using the Desktop Micro Computer Tomograph "µCT 40" and the Avance III NMR spectrometer.
By leveraging the insights and tools provided by PubCompare.ai, researchers can enhance the reproducibility and accuracy of their MS 180 experiments, leading to more reliable and impactful findings in the field of bioresearch.