Arabidopsis thaliana wild-type (ecotype Columbia) and mutant plants were grown in soil supplemented with Hoagland medium in growth chambers under long-day conditions (16 h light/8 h darkness) at 22 °C during the day and 20 °C during the night. The light intensity was set at 140 μE m−2 s−1. The 2-Cys Prx A–2-Cys Prx B double mutant, denoted Δ2cp, was obtained by manual crossing of the single mutants 2cpA, line SALK_065264, and 2cpB, line SALK_017213, previously characterized (Kirchsteiger et al., 2009 (link)). Seeds resulting from this cross were checked for heterozygosity of T-DNA insertions in the 2cpA and 2cpB genes. The plants were then selfed and double homozygous plants were detected in the progeny by PCR analysis of genomic DNA using oligonucleotides a (5′-GAGAAGTTGAACACCGA-3′) and b (5′-GGGGACAAAGTGAGAATC-3′) for the 2cpA gene, and a′ (5′-CCACCTGAACCAAGAAAG-3′) and b′ (5′-CCTGCAAGACAACATCAC-3′) for the 2cpB gene in conjunction with the oligonucleotide T (5′-TGGTTCACGTAGTGGGCCATCG-3′) located in the T-DNA. A T-DNA homozygous line SALK_128914 (Alonso et al., 2003 (link)) in the single gene encoding Trx x of Arabidopsis (At1g50320 locus) was selected by PCR analysis of genomic DNA with oligonucleotides c (5′-GCCATGGACTCTATCGTCTC-3′) and d (5′-CCTTCCCTTCTGCTCCCT-3′) in conjunction with the T oligonucleotide. The NTRC knock-out mutant was described previously (Serrato et al., 2004 (link)).
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M 140
M 140
M 140 is a Meshing Technique used in computational fluid dynamics and finite element analysis.
It involves the division of a continuous domain into a set of discrete subdomains, known as elements, to facilitate the numerical solution of partial differential equations.
This process enhances the accuracy and reliability of simulations by capturing the complex geometry and physics of the problem.
The M 140 method is particularly useful for modeling intricate shapes, fluid-structure interactions, and multiphysics problems across a wide range of engineering and scientific disciplines.
Its versatility and computational efficiency make it an indispensible tool for researchers and engineers seeking to enhance the reproducibility and accuracy of their work.
It involves the division of a continuous domain into a set of discrete subdomains, known as elements, to facilitate the numerical solution of partial differential equations.
This process enhances the accuracy and reliability of simulations by capturing the complex geometry and physics of the problem.
The M 140 method is particularly useful for modeling intricate shapes, fluid-structure interactions, and multiphysics problems across a wide range of engineering and scientific disciplines.
Its versatility and computational efficiency make it an indispensible tool for researchers and engineers seeking to enhance the reproducibility and accuracy of their work.
Most cited protocols related to «M 140»
Arabidopsis
Arabidopsis thalianas
Culture Media
Darkness
DNA, A-Form
Ecotype
Genes
Genome
Heterozygote
Homozygote
Insertion Mutation
Light
M 140
Oligonucleotides
Plant Embryos
Plants
1-naphthol-8-amino-3,6-disulfonic acid
Argon
Capillaries
Daughter
derivatives
Glycerophospholipids
Lipids
M 140
Mass Spectrometry
Phosphatidic Acid
Phosphatidylcholines
phosphatidylethanolamine
Phosphatidyl Glycerol
Phosphatidylserines
Phospholipids
Radionuclide Imaging
Retinal Cone
Spectrometry, Mass, Electrospray Ionization
Sphingomyelins
Tandem Mass Spectrometry
The IgG3 (glyco)peptides were analyzed with nanoLC-reversed phase (RP)-electrospray (ESI)-ion trap (IT)-MS(/MS) on an Ultimate 3000 RSLCnano system (Dionex/Thermo Scientific) coupled to an amaZon speed ESI-IT-MS (Bruker Daltonics, Bremen, Germany). A precolumn (Acclaim PepMap C18 capillary column, 300 μm x 5 mm, particle size 5 μm, Dionex/Thermo Scientific) was used to wash and concentrate the sample, and separation was achieved on an Acclaim PepMap RSLC C18 nanocolumn (75 μm x 150 mm, particle size 2 μm, Dionex/Thermo Scientific) with a flow rate of 500 nl/min. The following linear gradient was used, with solvent A consisting of 0.1% formic acid in water and solvent B of 95% acetonitrile, 5% water: t = 0 min, 1% solvent B; t = 5 min, 1% B; t = 20 min, 25% B; t = 25 min, 70% B; t = 30 min, 70% B; t = 31 min, 1% B; t = 55 min, 1% B. The sample was ionized in positive ion mode with an ESI-nanosprayer (4500 V) using a bare fused silica capillary (internal diameter of 20 μm). The solvent was evaporated at 180 °C with a nitrogen flow of 5 liters/min. A CaptiveSpray nanoBooster (Bruker Daltonics) was mounted onto the mass spectrometer and saturated the nitrogen flow with ACN to enhance the sensitivity. The MS1 ion detection window was set at m/z 350–1400, and the MS2 window at m/z 140–2200. The three highest nonsingly charged peaks in each MS1 spectrum were automatically fragmented through collision-induced dissociation (CID). In order to identify the peptide sequence of proteinase K- and trypsin-generated O-glycopeptides, MS3 analysis was performed on manually selected precursors: the MS2 peak representing the peptide without sugars attached was targeted for fragmentation. In a separate LC-MS run, electron transfer dissociation fragmentation was done on selected precursor ions.
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acetonitrile
Capillaries
Electron Transport
Endopeptidase K
formic acid
Glycopeptides
Hypersensitivity
IgG3
Ions
M 140
Nitrogen
Peptides
Silicon Dioxide
Solvents
Sugars
Tandem Mass Spectrometry
Trypsin
Z 350
Prototype Satellite Relay Data-Loggers (SRDLs, Sea Mammal Research Unit, University of St Andrews, Scotland) were attached to six adult female bearded seals (August 2011 N = 4; August 2012 N = 2) and 10 adult female ringed seals (August 2012 only), in Svalbard Norway. Programming details for telemetry devices are outlined in Supplementary Materials. All research activities including both animal care and field site permitting during this study were approved and carried out under permits from the Norwegian Animal Care Authority (Forsøksdyrutvalget ref. 2010/45416 and 2011/42085) and the Governor of Svalbard (Sysselmannen på Svalbard Ref. 2011/00488-52). In addition to the standard sensors for measuring dive data, each SRDL contained an Argos-linked Fastloc GPS transmitter. All tags were programmed to the same specifications (S1 File ), and the default speed parameter was used for the Argos Kalman filtering process (10ms-1). We are unaware of any other speed parameter setting being used in the marine mammal research community, and can thus not comment on the effects of varying this threshold with respect to the outcome of the Argos SRUKF process. Capturing and handling of these animals was conducted using the same methods as those outlined in [21 (link)]. Argos locations are derived as a by-product of all messages transmitted from the SRDL to the satellite system, while transmitted GPS data consist of a random subset of locations collected by the Fastloc GPS receiver on the animal, resulting in temporally decoupled Argos and GPS positions. Calibration studies of Fastloc GPS data show errors (at the 95th percentile level) between 24.2 m and 140 m for locations estimated by eight and five satellite acquisitions, respectively [22 ]. We removed all GPS locations with less than five satellite acquisitions, and henceforth assume the remaining GPS locations reflect the true position of the animal [23 (link)].
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Animals
M 140
Mammals
Marines
Medical Devices
Phocidae
Telemetry
Woman
All mutants used are in the Columbia (Col) wild-type accession of Arabidopsis thaliana. The ddm1-2 allele was described before [33] (link). A new lhp1 allele, lhp1-6, was identified in the SALK T-DNA insertion mutant collection (SALK_011762). LHP1 and lhp1-7 cDNAs were cloned into vector pK7FWG2 [34] (link), which was used to transform plants by floral dip with Agrobacterium tumefaciens (strain GV3101). Seeds were germinated on sterile basal salts Murashige and Skoog (MS) medium (Duchefa, Brussels, Belgium), and plants were analyzed on plates or transferred to soil 10 days after germination. Alternatively, seeds were directly sown on soil. Plants were kept in Conviron growth chambers with mixed cold fluorescent and incandescent light (110 to 140 µmol m−2 s−1, 21±2°C) under long day (LD, 16h light) or short day (SD, 8h light) photoperiods or were alternatively raised in green houses.
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Agrobacterium tumefaciens
Alleles
Arabidopsis thalianas
Cloning Vectors
Cold Temperature
DNA, Complementary
Germination
Incandescence
Light
like heterochromatin protein 1
M 140
Plant Embryos
Plants
Salts
Sterility, Reproductive
Strains
Most recents protocols related to «M 140»
The unicellular green alga C. reinhardtii strain CC-125 cells (1.5 × 106) were cultured in 50 mL liquid tris-acetate-phosphate (TAP) media in 250 mL flasks (Harris, 1989 ) by shaking at 25°C and 140 rpm under constant white light of 90–100 μmol photons m−2 s−1. In addition to the wild type (WT), two transgenic C. reinhardtii lines (AtTHI-OE1 and AtTHI-OE2) harboring the Arabidopsis thaliana Thionin 2.1 gene, which encodes antibacterial peptides, thionins, were used to investigate genotype-dependent radiation-sensitivity. Cells were harvested at 800 × g, dispensed, and subjected to X- or γ-irradiation as described below. The subsequent post-irradiation cultivations of the cells were performed in 10 mL fresh TAP media in 50 mL conical tubes, with an initial optical density of 0.05 at 750 nm for mock (or control) under the same culture conditions. The basal TAP medium was supplemented with 5 or 10 mM NaHCO3 to evaluate the synergistic effect of X-rays and sodium bicarbonate on cell growth.
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Acetate
Animals, Transgenic
Anti-Bacterial Agents
Arabidopsis thalianas
Bicarbonate, Sodium
Cells
G-800
Genes
Genotype
Light
M 140
Peptides
Phosphates
Radiation Tolerance
Radiotherapy
Strains
Thionins
Tromethamine
X-Rays, Diagnostic
Colloidal silica nanoparticles
of an average diameter of 50 nm were purchased from Nissan Inc. Two
types of nanoparticles were prepared: (1) particles with grafted PMMA
with a graft density of 0.34 chains/nm2 and a molecular
weight of 120 000 g/mol, (2) particles with grafted polyaniline
acrylate polymer at a graft density of 0.34 chains/nm2 and
a molecular weight of 134 000 g/mol.
To create the grafted
polymers, poly(methyl methacrylate) (PMMA) and poly(acrylic acid N-hyroxysuccinimide) (PNAS) were synthesized by surface-initiated
reversible addition-fragmentation chain transfer polymerization (SI-RAFT).
The RAFT agent was 2-(dodecylthiocarbonothioylthio) propanoic acid
(DoPAT). All chemicals were used as received unless otherwise specified.
Methyl methacrylate (MMA, 99%, Acros) was purified by filtration through
an activated basic alumina column. Azobisisobutyronitrile (AIBN) was
recrystallized from methanol before use. Molecular weights and dispersity
were determined by monitoring monomer conversion through 1H NMR and gel permeation chromatography (GPC). THF was used as the
eluent for GPC at 30 °C and a flow rate of 1.0 mL/min. GPC was
calibrated with poly(methyl methacrylate) (PMMA) standards obtained
from Polymer Laboratories.
To synthesize free polyaniline acrylate,
DoPAT (5 mg, 0.014 mmol),
NAS (0.482 g, 2.84 mmol), and AIBN (140 μL in 0.01 M solution)
were dispersed in 4.75 mL of DMF and transferred into a dried Schlenk
flask. The mixture was degassed by three freeze–pump–thaw
cycles, back-filled with nitrogen, and then placed in an oil bath
at 65 °C. The polymerization solution was quenched in an ice
bath and exposed to air after 24 h. The polymer solution was precipitated
into diethyl ether and centrifuged at 6000 rpm for 5 min. The dispersion-precipitation
process was repeated four times. The polymer was then redissolved
in 5 mL of DMF and sparged with nitrogen for 15 min. N-Phenyl-p-phenylenediamine (1.05 g, 5.6 mmol) was
dissolved in 2 mL of DMF. The solution was then added to the polymer
solution where it was then transferred to an oil bath at 110 °C
for 24 h. The polymerization was quenched in an ice bath and precipitated
into diethyl ether and centrifuged at 6000 rpm for 5 min. The polymer
was then dissolved in THF, and the dispersion-precipitation process
was repeated until the supernatant was colorless. Polyaniline-acrylate-grafted
NPs were synthesized by a surface-initiated reversible addition-fragmentation
chain transfer polymerization (SI-RAFT).15 (link) A typical polyaniline-acrylate-grafted NP synthesis was: DoPAT-NP
(0.05 g, σ = 0.34 chains/nm2), NAS (0.30 g, 1.77
mmol), and AIBN (18 μL in a 0.1 M solution) were dispersed in
5 mL of DMF and transferred to a Schlenk flask. The remaining procedure
is identical to the free polyaniline acrylate synthesis.
of an average diameter of 50 nm were purchased from Nissan Inc. Two
types of nanoparticles were prepared: (1) particles with grafted PMMA
with a graft density of 0.34 chains/nm2 and a molecular
weight of 120 000 g/mol, (2) particles with grafted polyaniline
acrylate polymer at a graft density of 0.34 chains/nm2 and
a molecular weight of 134 000 g/mol.
To create the grafted
polymers, poly(methyl methacrylate) (PMMA) and poly(acrylic acid N-hyroxysuccinimide) (PNAS) were synthesized by surface-initiated
reversible addition-fragmentation chain transfer polymerization (SI-RAFT).
The RAFT agent was 2-(dodecylthiocarbonothioylthio) propanoic acid
(DoPAT). All chemicals were used as received unless otherwise specified.
Methyl methacrylate (MMA, 99%, Acros) was purified by filtration through
an activated basic alumina column. Azobisisobutyronitrile (AIBN) was
recrystallized from methanol before use. Molecular weights and dispersity
were determined by monitoring monomer conversion through 1H NMR and gel permeation chromatography (GPC). THF was used as the
eluent for GPC at 30 °C and a flow rate of 1.0 mL/min. GPC was
calibrated with poly(methyl methacrylate) (PMMA) standards obtained
from Polymer Laboratories.
To synthesize free polyaniline acrylate,
DoPAT (5 mg, 0.014 mmol),
NAS (0.482 g, 2.84 mmol), and AIBN (140 μL in 0.01 M solution)
were dispersed in 4.75 mL of DMF and transferred into a dried Schlenk
flask. The mixture was degassed by three freeze–pump–thaw
cycles, back-filled with nitrogen, and then placed in an oil bath
at 65 °C. The polymerization solution was quenched in an ice
bath and exposed to air after 24 h. The polymer solution was precipitated
into diethyl ether and centrifuged at 6000 rpm for 5 min. The dispersion-precipitation
process was repeated four times. The polymer was then redissolved
in 5 mL of DMF and sparged with nitrogen for 15 min. N-Phenyl-p-phenylenediamine (1.05 g, 5.6 mmol) was
dissolved in 2 mL of DMF. The solution was then added to the polymer
solution where it was then transferred to an oil bath at 110 °C
for 24 h. The polymerization was quenched in an ice bath and precipitated
into diethyl ether and centrifuged at 6000 rpm for 5 min. The polymer
was then dissolved in THF, and the dispersion-precipitation process
was repeated until the supernatant was colorless. Polyaniline-acrylate-grafted
NPs were synthesized by a surface-initiated reversible addition-fragmentation
chain transfer polymerization (SI-RAFT).15 (link) A typical polyaniline-acrylate-grafted NP synthesis was: DoPAT-NP
(0.05 g, σ = 0.34 chains/nm2), NAS (0.30 g, 1.77
mmol), and AIBN (18 μL in a 0.1 M solution) were dispersed in
5 mL of DMF and transferred to a Schlenk flask. The remaining procedure
is identical to the free polyaniline acrylate synthesis.
1H NMR
4-aminodiphenylamine
acrylate
Anabolism
azobis(isobutyronitrile)
Bath
Ethyl Ether
Filtration
Freezing
Gel Chromatography
M 140
Methanol
Methylmethacrylate
Nitrogen
Oxide, Aluminum
Peptide Nucleic Acids
polyacrylic acid
polyaniline
Polymerization
Polymers
Polymethyl Methacrylate
propionic acid
Silicon Dioxide
Using time-dependent two-phase flow physics, the finite element simulations of a 2D droplet on a moving plate are performed in COMSOL Multiphysics 5.6. Navier-Stokes equations are solved in the liquid and air domain. Liquid/air/solid interfaces are modeled using the level-set method. Before prescribing the motion to the plate, the droplet is allowed to equilibrate on the stationary plate to achieve its equilibrium shape based on the prescribed contact angle. Following equilibration, the plate is prescribed a sinusoidal displacement using a moving mesh interface, where it is modeled as a moving boundary within a deforming domain. Automatic remeshing of the domain is performed at specified timesteps to prevent excessive deformation of the mesh elements because of the moving boundary. For the outer boundaries of the domain, we prescribed the outlet boundary condition, specifying the static pressure to zero. For the wetted wall, i.e., the surface of the plate, we defined a static contact angle with a Navier-slip equal to the maximum size of the mesh element. We used a free triangular mesh with a maximum element size of 0.015 mm and a minimum of 0.0001 mm. The reinitialization parameter for the level set method is set to 0.5 m/s, and the parameter controlling interface thickness is equal to the mesh element’s maximum size. We simulated droplets at different contact angles ranging from 100∘–180∘. For 2D simulations, we fixed the area of the droplet corresponding to the droplet’s diameter of 1 mm, forming a perfect circle and using this same area to equilibrate droplets under gravity at different contact angles. Given no coupling between the upper and lower springs (Supplementary Information, Section II , B), we prescribed the sinusoidal motion to the plate of the form where f is the frequency of plate at a constant peak acceleration of 140 m/s2 with the frequencies of vibration ranging from 50 Hz to 300 Hz. We have also performed simulations for droplet sizes 1.2 mm and 1.4 mm, and for acceleration 80 m/s2 which show good match with the drop-on-plate experiments (Fig. 2 and Supplementary Fig. 10) . However, we didn’t find significant differences between the superpropulsion curves when compared with a droplet of 1 mm size.
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Acceleration
Gravity
M 140
Natural Springs
Pressure
Sinusoidal Beds
Vibration
The Saccharomyces cerevisiae strains used are all BY4741 derivative and are listed in Table S1 . To generate cdh1∆::HIS3 strain, cdh1∆::KanMX4 was transformed with a DNA fragment containing HIS3MX. To construct double mutant strains, the DNA fragment containing cdh1∆::HIS3 was amplified and transformed in the deletion strains. To generate Rpn4-HAcdh1Δ::kan strain, Rpn4-HA:HIS3 was transformed with a DNA fragment containing cdh1∆::KanMX4. Strains were transformed by the standard lithium acetate procedure [59 (link)]. Gene deletion was confirmed by PCR. For overexpression of Cdh1-m11 and Sod2p, cells were transformed with the plasmids pRS416-GALL-3HA-Cdh1-m11 [26 (link)] and Yep352-SOD2 [45 (link)], respectively.
Cells were grown in rich medium [YPGal: 2% (w/v) galactose, 1% (w/v) yeast extract, 2% (w/v) bactopeptone] or synthetic complete medium [SC: 0.67% (w/v) Bacto-yeast nitrogen base w/o amino acids, 2% (w/v) glucose and 0.2% (w/v) Dropout mix] lacking uracil/leucine, as appropriate. For Cdh1-m11 overexpression, cells were grown in YPRaff medium [2% (w/v) raffinose, 1% (w/v) yeast extract, 2% (w/v) bactopeptone] overnight until mid-log phase and cultured with 4% galactose for 3h before oxygen consumption analysis. Cultures were routinely grown at 26 °C in an orbital shaker at 140 r.p.m.
Cells were grown in rich medium [YPGal: 2% (w/v) galactose, 1% (w/v) yeast extract, 2% (w/v) bactopeptone] or synthetic complete medium [SC: 0.67% (w/v) Bacto-yeast nitrogen base w/o amino acids, 2% (w/v) glucose and 0.2% (w/v) Dropout mix] lacking uracil/leucine, as appropriate. For Cdh1-m11 overexpression, cells were grown in YPRaff medium [2% (w/v) raffinose, 1% (w/v) yeast extract, 2% (w/v) bactopeptone] overnight until mid-log phase and cultured with 4% galactose for 3h before oxygen consumption analysis. Cultures were routinely grown at 26 °C in an orbital shaker at 140 r.p.m.
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Amino Acids, Basic
Bacto-peptone
CDH1 protein, human
Cells
Deletion Mutation
Galactose
Gene Deletion
Glucose
Leucine
lithium acetate
M 140
Nitrogen
Oxygen Consumption
Plasmids
Raffinose
Saccharomyces cerevisiae
SOD2 protein, human
Strains
Uracil
Pilot-scale cultures were carried out in three identical single-use ‘hanging-bag’ (HB) photobioreactors (PBR) [29 (link)]. Each PBR was made from heat-sealed polythene layflat tubing (1000-gauge, UK packing, London, UK) with a width of 10.2 cm and a final working volume of 5 L. A late logarithmic-phase culture was used to inoculate the HBs to an initial optical density (OD) reading of 0.015 at 750 nm. The cells were grown in a temperature-controlled room at 24.5 °C under constant illumination provided by three light-emitting diode (LED) panels with an average light intensity of 140 µmol.m−2.s−1. The cultures were aerated and recirculated using a constant air flowrate of 1 L/min. No carbon dioxide was supplemented. The growth was monitored by off-line OD750 readings using semi-micro acrylic cuvettes with a path length of 10 mm and fresh TAP medium as blank.
The cultures were harvested after 3 days upon reaching the end of the logarithmic phase. Before harvesting, each HB was sampled for dry cell weight (DCW) measurements and immunoblotting (biological triplicates). The pellets for DCW were obtained from 50 mL samples after centrifugation (5000 g, 10 min, 12 °C) and stored at –20 °C for future freeze drying. For immunoblotting, 10 mL samples were centrifuged as previously described, snap-frozen in liquid nitrogen and stored at –80 °C for later analyses.
The cultures were harvested after 3 days upon reaching the end of the logarithmic phase. Before harvesting, each HB was sampled for dry cell weight (DCW) measurements and immunoblotting (biological triplicates). The pellets for DCW were obtained from 50 mL samples after centrifugation (5000 g, 10 min, 12 °C) and stored at –20 °C for future freeze drying. For immunoblotting, 10 mL samples were centrifuged as previously described, snap-frozen in liquid nitrogen and stored at –80 °C for later analyses.
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Biopharmaceuticals
Carbon dioxide
Centrifugation
Freezing
Light
Lighting
M 140
Nitrogen
Pellets, Drug
Photobioreactors
Polyethylene
Top products related to «M 140»
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The Acclaim PepMap 100 C18 column is a high-performance liquid chromatography (HPLC) column designed for the separation and analysis of peptides. It features a reversed-phase C18 stationary phase and a 100 Å pore size, which makes it suitable for the separation of complex peptide mixtures.
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The QIAGEN QIAamp® DNA Blood Mini and Midi Kits are designed for the rapid and efficient purification of genomic DNA from whole blood, plasma, serum, buffy coat, and other liquid sample types. The kits utilize a silica-membrane-based technology to isolate high-quality DNA that is suitable for a variety of downstream applications.
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FlexImaging 4.1 is a software solution for mass spectrometry imaging. It provides data acquisition and processing capabilities for MALDI-MS imaging experiments.
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The PepMap C18 is a reversed-phase liquid chromatography column designed for the separation and analysis of peptides. It features a silica-based, spherical packing material with a C18 bonded phase. This column is suitable for applications in proteomics and other areas requiring the separation and characterization of peptides.
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The Nucleoside Digestion Mix is a laboratory reagent designed to break down nucleosides into their individual components. It contains a combination of enzymes and buffers that facilitate the hydrolysis of nucleosides into their respective nucleobases, sugars, and phosphate groups.
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More about "M 140"
Mesh technique, computational fluid dynamics, finite element analysis, numerical simulation, partial differential equations, complex geometry, fluid-structure interactions, multiphysics problems, engineering, scientific research, reproducibility, accuracy, Q Exactive Plus, Acclaim PepMap 100 C18 column, QIAGEN QIAamp®DNA blood mini and midi kits, Q Exactive Orbitrap, Brucella Broth media, FlexImaging 4.1, PepMap C18, Nucleoside Digestion Mix, 6490A Triple Quadrupole Mass Detector, XSelect HSS T3 XP column.
The M 140 meshing technique is a powerful tool used in computational fluid dynamics and finite element analysis to enhance the accuracy and reliability of numerical simulations.
By dividing a continuous domain into discrete subdomains, known as elements, the M 140 method can effectively capture the complex geometry and physics of a problem, enabling researchers and engineers to model intricate shapes, fluid-structure interactions, and multiphysics scenarios across a wide range of disciplines.
This versatile and computationally efficient approach is indispensible for improving the reproducibility and accuracy of scientific research and engineering applications, making it a crucial component in workflows that leverage advanced analytical technologies like the Q Exactive Plus, Acclaim PepMap 100 C18 column, QIAGEN QIAamp®DNA blood mini and midi kits, Q Exactive Orbitrap, Brucella Broth media, FlexImaging 4.1, PepMap C18, Nucleoside Digestion Mix, 6490A Triple Quadrupole Mass Detector, and XSelect HSS T3 XP column.
The M 140 meshing technique is a powerful tool used in computational fluid dynamics and finite element analysis to enhance the accuracy and reliability of numerical simulations.
By dividing a continuous domain into discrete subdomains, known as elements, the M 140 method can effectively capture the complex geometry and physics of a problem, enabling researchers and engineers to model intricate shapes, fluid-structure interactions, and multiphysics scenarios across a wide range of disciplines.
This versatile and computationally efficient approach is indispensible for improving the reproducibility and accuracy of scientific research and engineering applications, making it a crucial component in workflows that leverage advanced analytical technologies like the Q Exactive Plus, Acclaim PepMap 100 C18 column, QIAGEN QIAamp®DNA blood mini and midi kits, Q Exactive Orbitrap, Brucella Broth media, FlexImaging 4.1, PepMap C18, Nucleoside Digestion Mix, 6490A Triple Quadrupole Mass Detector, and XSelect HSS T3 XP column.