We performed a laboratory analysis to construct an experimental dataset of proteins from a Gram-negative bacterium, Pseudomonas aeruginosa PA01, which was used to assess PSORTb 2.0, PSORTb 3.0, PA 2.5 and PA 3.0. This represents an independent dataset that includes hypothetical and uncharacterized proteins with previously unknown SCLs. P.aeruginosa is a bacterium noted for its diverse metabolic capacity and large genome/proteome size, and so represents an excellent organism with which to generate such a dataset (Stover et al., 2000 (link)). To generate this experimental dataset, we extracted protein samples from the cytoplasmic, periplasmic and secreted fractions of P.aeruginosa PA01. The resulting proteins in each fraction were digested to peptides and differentially labeled using formaldehyde isotopologues (Chan and Foster, 2008 (link)) prior to analysis by liquid chromatography–tandem mass spectrometry (LC–MS/MS), exactly as previously described (Chan et al., 2006 (link)). Abundance ratios between SCL were calculated using MSQuant (http://msquant.sourceforge.net/ ). To ensure a high-quality dataset with minimal contaminating proteins from other subcellular compartments, proteins that were only found in the cytoplasmic fraction and never in the other two soluble fractions were used to assess PSORTb 3.0 and PA 3.0 prediction results. This dataset was also felt to be most appropriate for assessment, since our analysis had suggested that most proteins of previously unknown localization in the old version of PSORTb were most likely cytoplasmic proteins. Further details on the experimental protocols for this proteomics analysis of the subcellular fractions can be found in Supplementary Material—methods for mass spectrometry protein identification.
>
Procedures
>
Laboratory Procedure
>
Spectrometry
Spectrometry
Spectrometry is a powerful analytical technique that enables the identification and quantification of chemical compounds by measuring the interaction between matter and electromagnetic radiation.
This non-destructive method can be applied to a wide range of samples, from biological macromolecules to complex industrial mixtures.
Spectrometric techniques involve the separation of light into its constituent wavelengths, followed by the detection and analysis of the resulting spectrum.
These measurements provide valuable information about the chemical composition, structure, and properties of the analyte.
Spectrometry plays a crucial role in fields such as chemistry, physics, biology, and environmental science, facilitating advanced research, quality control, and diagnostic applications.
With continual advancements in instrumentation and data analysis, spectrometry remains an indispensable tool for scientists seeking to unveil the secrets of the physical world.
This non-destructive method can be applied to a wide range of samples, from biological macromolecules to complex industrial mixtures.
Spectrometric techniques involve the separation of light into its constituent wavelengths, followed by the detection and analysis of the resulting spectrum.
These measurements provide valuable information about the chemical composition, structure, and properties of the analyte.
Spectrometry plays a crucial role in fields such as chemistry, physics, biology, and environmental science, facilitating advanced research, quality control, and diagnostic applications.
With continual advancements in instrumentation and data analysis, spectrometry remains an indispensable tool for scientists seeking to unveil the secrets of the physical world.
Most cited protocols related to «Spectrometry»
Bacteria
Cytoplasm
Feelings
Formaldehyde
Gram Negative Bacteria
Liquid Chromatography
Mass Spectrometry
Peptides
Periplasm
Proteins
Proteome
Proto-Oncogene Mas
Pseudomonas aeruginosa
Spectrometry
Staphylococcal Protein A
Subcellular Fractions
Tandem Mass Spectrometry
Cells
Chloroform
Isopropyl Alcohol
Lipids
Mass Spectrometry
Methanol
methylene dimethanesulfonate
Pressure
Spectrometry
Tandem Mass Spectrometry
As input, proteiNorm
expects tab-separated peptide (optional) and protein data (not on
logarithmic scale) as produced by software such as MaxQuant,9 (link) where each row represents a peptide or protein
and the column names of the measured intensities (samples) beginning
with “Reporter intensity corrected” followed by an integer
and an optional label (e.g., “Reporter intensity corrected
5 TMT2”) for TMT experiments. The column names for samples
in label-free experiments should begin with “Intensity”
followed by an integer (“Intensity 01”). Data from both
mass spectrometry quantitation methods, tandem mass tag (TMT) and
label-free mass spectrometry, are supported. The TMT reporter intensities
should be corrected using the error correction factors provided by
Thermo Fisher for the specific TMT lot that was used during the sample
preparation. These correction factors are imported into MaxQuant when
setting up the database search parameters. The MaxQuant “proteinGroups.txt”
output file will then contain column names for each TMT reporter ion
labeled as “Reporter intensity corrected” and “Reporter
intensity”. In the following examples, we are using the “Reporter
intensity corrected” columns from MaxQuant since these intensities
apply the TMT correction factors. The reporter ion isotopic distributions
(−2, −1, +1, +2) are primarily for carbon isotopes with
reporter ion interference for each mass tag. ProteiNorm automatically
detects these column names and determines if the data is TMT or label-free
data type. ProteiNorm also removes proteins flagged as common contaminants
and reverse sequences in the MaxQuant output using the column names
“Potential contaminant” and “Reverse”
provided in the proteinGroups.txt MaxQuant output file. If you prefer
to load in a different matrix of data, then the column labels for
the samples will need to be modified to match the naming structure
provided here. An example of the data input files is hosted on Github
for both TMT and label-free data sets.
Due to the detection
limits of mass spectrometry instruments, many measurements of peptides
or proteins result in intensity levels of zero. These values will
be considered as missing values (denoted as NA) and can be imputed
with precaution. A modified heatmap of missing values (Figure 2 C) from the DEP Bioconductor
package10 (link) helps to determine if data is
missing at random (MAR) or missing not at random (MNAR), and the MSnbase
vignette describes different imputation methods used for different
types of missing data.11 (link)
expects tab-separated peptide (optional) and protein data (not on
logarithmic scale) as produced by software such as MaxQuant,9 (link) where each row represents a peptide or protein
and the column names of the measured intensities (samples) beginning
with “Reporter intensity corrected” followed by an integer
and an optional label (e.g., “Reporter intensity corrected
5 TMT2”) for TMT experiments. The column names for samples
in label-free experiments should begin with “Intensity”
followed by an integer (“Intensity 01”). Data from both
mass spectrometry quantitation methods, tandem mass tag (TMT) and
label-free mass spectrometry, are supported. The TMT reporter intensities
should be corrected using the error correction factors provided by
Thermo Fisher for the specific TMT lot that was used during the sample
preparation. These correction factors are imported into MaxQuant when
setting up the database search parameters. The MaxQuant “proteinGroups.txt”
output file will then contain column names for each TMT reporter ion
labeled as “Reporter intensity corrected” and “Reporter
intensity”. In the following examples, we are using the “Reporter
intensity corrected” columns from MaxQuant since these intensities
apply the TMT correction factors. The reporter ion isotopic distributions
(−2, −1, +1, +2) are primarily for carbon isotopes with
reporter ion interference for each mass tag. ProteiNorm automatically
detects these column names and determines if the data is TMT or label-free
data type. ProteiNorm also removes proteins flagged as common contaminants
and reverse sequences in the MaxQuant output using the column names
“Potential contaminant” and “Reverse”
provided in the proteinGroups.txt MaxQuant output file. If you prefer
to load in a different matrix of data, then the column labels for
the samples will need to be modified to match the naming structure
provided here. An example of the data input files is hosted on Github
for both TMT and label-free data sets.
Due to the detection
limits of mass spectrometry instruments, many measurements of peptides
or proteins result in intensity levels of zero. These values will
be considered as missing values (denoted as NA) and can be imputed
with precaution. A modified heatmap of missing values (
package10 (link) helps to determine if data is
missing at random (MAR) or missing not at random (MNAR), and the MSnbase
vignette describes different imputation methods used for different
types of missing data.11 (link)
Carbon Isotopes
Isotopes
Mass Spectrometry
Peptides
Proteins
Spectrometry
acylcarnitine
Amino Acids
Bile Acids
Biogenic Amines
Biological Assay
Carnitine
Clinical Laboratory Services
Edetic Acid
Ergocalciferol
Flow Injection Analysis
Hexoses
Homo sapiens
Hypersensitivity
Isotopes
Lipid A
Parathyroid Hormone
Peptides
Phosphatidylcholines
Plasma
Serum
Spectrometry
Sphingomyelins
Tandem Mass Spectrometry
Cells
Mass Spectrometry
Plasma
Protoplasm
Pyroptosis
Spectrometry
Tissue, Membrane
Vision
Yttrium
Most recents protocols related to «Spectrometry»
Example 4
Octadecanoate Functionalized Core (IMS 018 H)
To a round bottom flask was added one or more of the following “core” compounds: tripentaerythritol (“H”) made from the above cores. These were dissolved in tetrahydrofuran. 1.1 molar equivalents (per —OH of the hydroxyl terminated cores or dendrimers) of Octadecanoic Acid were added to the solution of cores. To these reagents were added 1.2 molar equivalents (per —OH of the hydroxyl terminated cores or dendrimers) of dicyclohexylcarbodiimide and 0.1 molar equivalents (per —OH of hydroxyl-terminated core or of dendrimer) of 4-dimethylaminopyridine (DMAP).
The reaction mixture was stirred vigorously for approximately 12 hours at standard temperature and pressure. The reaction was monitored by MALDI-TOF MS to determine completion of the reaction for each of the cores present in the reaction. After complete esterification is observed by MALDI-TOF MS, the flask contents were transferred to a separatory funnel, diluted with dichloromethane, extracted twice with 1M aqueous NaHSO4 (sodium bisulfate) and extracted twice with 1M aqueous NaHCO3 (sodium bicarbonate). The organic layer was reduced in vacuo to concentrate the sample. A MALDI-TOF MS spectra of the purified product confirmed the purity of the mixture of esterified products and is shown in
4-dimethylaminopyridine
Bicarbonate, Sodium
Chromatography
Dendrimers
Dicyclohexylcarbodiimide
Esterification
Hydroxyl Radical
Methylene Chloride
Molar
Pressure
sodium bisulfate
Spectrometry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Stearates
stearic acid
tetrahydrofuran
Example 7
Benzoate Functionalized Cores (IMS 100 C-F)
To a round bottom flask was added one or more of the following “core” compounds: tris(hydroxymethyl)ethane (“C”), pentaerythritol (“D”), xylitol (“E”), dipentaerythritol (“F”) made from the above cores. These were dissolved in tetrahydrofuran. 1.1 molar equivalents (per —OH of the hydroxyl terminated cores or dendrimers) of Benzoic Acid were added to the solution of cores. To these reagents were added 1.2 molar equivalents (per —OH of the hydroxyl terminated cores or dendrimers) of dicyclohexylcarbodiimide and 0.1 molar equivalents (per —OH of hydroxyl-terminated core or of dendrimer) of 4-dimethylaminopyridine (DMAP).
The reaction mixture was stirred vigorously for approximately 12 hours at standard temperature and pressure. The reaction was monitored by MALDI-TOF MS to determine completion of the reaction for each of the cores present in the reaction. After complete esterification is observed by MALDI-TOF MS, the flask contents were transferred to a separatory funnel, diluted with dichloromethane, extracted twice with 1M aqueous NaHSO4 (sodium bisulfate) and extracted twice with 1M aqueous NaHCO3 (sodium bicarbonate). The organic layer was reduced in vacuo to concentrate the sample. A MALDI-TOF MS spectra of the purified product confirmed the purity of the mixture of esterified products and is shown in
4-dimethylaminopyridine
Benzoate
Benzoic Acid
Bicarbonate, Sodium
Chromatography
Dendrimers
Dicyclohexylcarbodiimide
Esterification
Ethane
Hydroxyl Radical
Methylene Chloride
Molar
pentaerythritol
Pressure
sodium bisulfate
Spectrometry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
tetrahydrofuran
Tromethamine
Xylitol
The solid catalyst was collected
from the water suspension by filtration under vacuum. The filter paper
with the black paste was dried at 20 °C by the airflow in a fume
hood. No inert gas protection was involved for catalyst handling or
transportation. The Ru and Pd contents in the catalysts were measured
by inductively coupled plasma–optical emission spectrometry
(ICP-OES, PerkinElmer Optima 8300) after digestion at the Microanalysis
Laboratory, University of Illinois at Urbana-Champaign. The oxidation
state of Ru and Pd was characterized by X-ray photoelectron spectroscopy
(XPS, Kratos AXIS Supra). The sp2 C 1s peak (284.5 eV)
of the carbon support was used for binding energy (BE) calibration.
XPS spectra in the resolution of 0.1 eV were fitted using CasaXPS
(version 2.3.19). Microscopic characterization was conducted using
scanning transmission electron microscopy (STEM, FEI Titan Themis
300) equipped with an energy-dispersive X-ray spectrometer (EDS) system.
The catalyst powder was resuspended and sonicated in distilled water
to further reduce the size. The STEM images were acquired with a high-angle
annular dark-field (HAADF) detector. Nano Measurer software package
was used for the statistical analysis of average particle size in
the STEM images. The specific surface areas of Ru and Pd were determined
by CO pulse titration experiments on a Quantachrome Autosorb-iQ physisorption–chemisorption
instrument. The calculation of metal dispersion used the surface Ru:CO
and Pd:CO stoichiometry of 12:741 (link) and 2:1,42 (link) respectively.
from the water suspension by filtration under vacuum. The filter paper
with the black paste was dried at 20 °C by the airflow in a fume
hood. No inert gas protection was involved for catalyst handling or
transportation. The Ru and Pd contents in the catalysts were measured
by inductively coupled plasma–optical emission spectrometry
(ICP-OES, PerkinElmer Optima 8300) after digestion at the Microanalysis
Laboratory, University of Illinois at Urbana-Champaign. The oxidation
state of Ru and Pd was characterized by X-ray photoelectron spectroscopy
(XPS, Kratos AXIS Supra). The sp2 C 1s peak (284.5 eV)
of the carbon support was used for binding energy (BE) calibration.
XPS spectra in the resolution of 0.1 eV were fitted using CasaXPS
(version 2.3.19). Microscopic characterization was conducted using
scanning transmission electron microscopy (STEM, FEI Titan Themis
300) equipped with an energy-dispersive X-ray spectrometer (EDS) system.
The catalyst powder was resuspended and sonicated in distilled water
to further reduce the size. The STEM images were acquired with a high-angle
annular dark-field (HAADF) detector. Nano Measurer software package
was used for the statistical analysis of average particle size in
the STEM images. The specific surface areas of Ru and Pd were determined
by CO pulse titration experiments on a Quantachrome Autosorb-iQ physisorption–chemisorption
instrument. The calculation of metal dispersion used the surface Ru:CO
and Pd:CO stoichiometry of 12:741 (link) and 2:1,42 (link) respectively.
Carbon
Digestion
Epistropheus
Filtration
Metals
Microscopy
Noble Gases
Pastes
Plasma
Powder
Pulse Rate
Radiography
Spectrometry
Stem, Plant
Titrimetry
Transmission Electron Microscopy
Vacuum
Vision
All the
chemicals were purchased
from Sigma-Aldrich, Merk, Fisher
Scientific, or VWR and used as received. DOTA was purchased from MacrocyclicsTM.
DO2A-DipyNox is adopted from our previous studies,32 (link),33 (link) and was synthesized by Dr. Liu (present address: Fu Jen Catholic
University, New Taipei City, Taiwan). Solvents were purchased from
Honeywell, BIOSOLVE or Aldrich and stored over 3 Å molecular
sieves before use. Traces of water from reagents were removed by co-evaporation
with toluene in reactions that required anhydrous conditions. Flash
chromatography was performed on Screening Devices silica gel 60 (40–63
μm) and C18-reversed phase silica gel (fully endcapped, 40–63
μm). LC–MS analysis was performed on a Surveyor HPLC
system (Thermo Finnigan) equipped with a C18 column (Gemini, 4.6 mm
× 50 mm, 5 μm particle size, Phenomenex), coupled to an
LCQ Advantage Max (Thermo Finnigan) ion-trap spectrometer (ESI+).
Thin-layer chromatography (TLC) analysis was performed on a silica
gel (F 1500 LS 254 Schleicher and Schuell, Dassel, Germany), which
was visualized by UV and/or ninhydrin, KMnO4. Reactions
were monitored by LC–MS analysis and TLC analysis. Waters preparative
HPLC system, equipped with a Waters C18-Xbridge 5 μm OBD (30
× 150 mm2) column, was used for purification, and
the applied buffers were H2O (2% TFA) and ACN. High-resolution
mass spectrometry analysis was performed with an LTQ Orbitrap mass
spectrometer (Thermo Finnigan), equipped with an electron spray ion
source in a positive mode (source voltage 3.5 kV, sheath gas flow
10 mL/min, and capillary temperature 250 °C) with resolution R = 60,000 at m/z 400
(mass range m/z = 150–2000)
and dioctyl phthalate (m/z = 391.284)
as a “lock mass.” NMR spectra were recorded on a Bruker
AV-400 (400.130/100.613 MHz), AV-500 (500.130/125.758 MHz), or AV-HDIII-600
(600.130/150.903 MHz) spectrometer. Chemical shifts (δ) are
reported in ppm relative to the residual signal of the deuterated
solvent.
chemicals were purchased
from Sigma-Aldrich, Merk, Fisher
Scientific, or VWR and used as received. DOTA was purchased from MacrocyclicsTM.
DO2A-DipyNox is adopted from our previous studies,32 (link),33 (link) and was synthesized by Dr. Liu (present address: Fu Jen Catholic
University, New Taipei City, Taiwan). Solvents were purchased from
Honeywell, BIOSOLVE or Aldrich and stored over 3 Å molecular
sieves before use. Traces of water from reagents were removed by co-evaporation
with toluene in reactions that required anhydrous conditions. Flash
chromatography was performed on Screening Devices silica gel 60 (40–63
μm) and C18-reversed phase silica gel (fully endcapped, 40–63
μm). LC–MS analysis was performed on a Surveyor HPLC
system (Thermo Finnigan) equipped with a C18 column (Gemini, 4.6 mm
× 50 mm, 5 μm particle size, Phenomenex), coupled to an
LCQ Advantage Max (Thermo Finnigan) ion-trap spectrometer (ESI+).
Thin-layer chromatography (TLC) analysis was performed on a silica
gel (F 1500 LS 254 Schleicher and Schuell, Dassel, Germany), which
was visualized by UV and/or ninhydrin, KMnO4. Reactions
were monitored by LC–MS analysis and TLC analysis. Waters preparative
HPLC system, equipped with a Waters C18-Xbridge 5 μm OBD (30
× 150 mm2) column, was used for purification, and
the applied buffers were H2O (2% TFA) and ACN. High-resolution
mass spectrometry analysis was performed with an LTQ Orbitrap mass
spectrometer (Thermo Finnigan), equipped with an electron spray ion
source in a positive mode (source voltage 3.5 kV, sheath gas flow
10 mL/min, and capillary temperature 250 °C) with resolution R = 60,000 at m/z 400
(mass range m/z = 150–2000)
and dioctyl phthalate (m/z = 391.284)
as a “lock mass.” NMR spectra were recorded on a Bruker
AV-400 (400.130/100.613 MHz), AV-500 (500.130/125.758 MHz), or AV-HDIII-600
(600.130/150.903 MHz) spectrometer. Chemical shifts (δ) are
reported in ppm relative to the residual signal of the deuterated
solvent.
Buffers
Capillaries
Diethylhexyl Phthalate
Electrons
Medical Devices
Ninhydrin
Silica Gel
Solvents
Spectrometry
tetraxetan
Thin Layer Chromatography
Toluene
| Reagent/resource | Reference or source | Identifier or catalog |
|---|---|---|
| Mycobacterium bovis BCG Pasteur | American Type Culture Collection | ATCC 35748 |
| M. bovis BCG gltBD transposon mutant | VIB – Vlaams Instituut voor Biotechnologie | (BCG_3922c TnInsertion‐8654) |
| Middlebrook 7H11 | Merck Life Science | M0428‐500G |
| Middlebrook 7H9 | Merck Life Science | M0178‐500G |
| OADC | Becton Dickenson | 212351 (4312351) |
| Glycerol | Merck Life Science | G7893‐1 L |
| Tyloxapol | Merck Life Science | T8761‐50G |
| Brain heart infusion agar | Merck Life Science | 70138‐500G |
| Rosins minimal media | Beste et al (2011 (link)) | N/A |
| [13C3] glycerol, 99% purity | CK Isotopes | CLM‐1510‐5 |
| [15N1] NH4Cl, 98% atom purity | Merck Life Science | 299251 |
| 2 liter bioreactor | Electrolab | Fermac 310/60 |
| Peristaltic pump | Rainin Rabbit Plus | N/A |
| Gas analyzer | Electrolab | Fermac 368 |
| Glycerol assay kit | Merck Life Science | MAK117 |
| Ammonia assay kit | Merck Life Science | MAK310 |
| BCA assay kit | Merck Life Science | 71285‐M |
| Ziehl neelsen stain | Merck Life Science | 1.09215 |
| tert‐butyldimethyl silyl chloride (TBDMSCl) | Merck Life Science | 00942‐10ML |
| N‐Methyl‐N‐(trimethylsilyl)trifluoroacetamide, MSTFA | Merck Life Science | M‐132 |
| GC–MS 7890‐5795 | Agilent | Borah et al (2019 (link)) |
| VF‐5 ms 30 m × 0.25 mm × 0.25 μm + 10 m EZ‐Guard | Agilent | CP9013 |
| Dionex UltiMate system (HPLC) | Thermo Fisher Scientific | 3000 RSLC |
| C18 and ZIC‐pHILIC column (150 mm × 4.6 mm, 5 μm column) | Merck Sequant | 150461 |
| Thermo Orbitrap Q Exactive Plus | Thermo Fisher Scientific | N/A |
| Chemstation | Agilent | N/A |
| GraphPad Prism 8.0 | GraphPad software | N/A |
| Omix v.2.0.7 | Omix Visualization GmbH & Co.KG, Lennestadt/Germany | N/A |
| 13CFLUX2 v2.2 | Weitzel et al (2013 (link)) | N/A |
| HOPS v2.0.0 | Jadebeck et al (2021 (link)) | N/A |
Biological Assay
Chlorides
Glycerin
Heart
High-Performance Liquid Chromatographies
Jumping Genes
prisma
Rabbits
Spectrometry
TBDMSCl
trifluoroacetamide
Top products related to «Spectrometry»
Sourced in Japan, United States, China, Germany, United Kingdom, Spain, Canada, Czechia
The S-4800 is a high-resolution scanning electron microscope (SEM) manufactured by Hitachi. It provides a range of imaging and analytical capabilities for various applications. The S-4800 utilizes a field emission electron gun to generate high-quality, high-resolution images of samples.
Sourced in United States, Germany, Japan, Singapore
The Optima 8300 is an inductively coupled plasma optical emission spectrometer (ICP-OES) designed for multi-element analysis. It provides high-performance elemental analysis across a wide range of concentrations and sample types.
Sourced in United States, Germany, Japan, United Kingdom
The Optima 5300 DV is an inductively coupled plasma optical emission spectrometer (ICP-OES) manufactured by PerkinElmer. It is designed for the analysis of a wide range of elements in various sample types, including environmental, geological, and industrial samples. The Optima 5300 DV utilizes dual-view technology, allowing for both axial and radial plasma viewing to provide enhanced sensitivity and detection limits.
Sourced in Germany, United States, Japan, United Kingdom, China, France, India, Greece, Switzerland, Italy
The D8 Advance is a versatile X-ray diffractometer (XRD) designed for phase identification, quantitative analysis, and structural characterization of a wide range of materials. It features advanced optics and a high-performance detector to provide accurate and reliable results.
Sourced in United States, China, Canada
The DU530 UV/VIS spectrophotometer is a laboratory instrument designed to measure the absorption or transmission of light by a sample across a range of ultraviolet and visible wavelengths. It is capable of performing quantitative and qualitative analysis of various chemical and biological samples.
Sourced in United States, China, Japan, Germany, United Kingdom, Canada, France, Italy, Australia, Spain, Switzerland, Netherlands, Belgium, Lithuania, Denmark, Singapore, New Zealand, India, Brazil, Argentina, Sweden, Norway, Austria, Poland, Finland, Israel, Hong Kong, Cameroon, Sao Tome and Principe, Macao, Taiwan, Province of China, Thailand
TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.
Sourced in United States, United Kingdom, Japan, China, Germany, Netherlands, Switzerland, Portugal
The ESCALAB 250Xi is a high-performance X-ray photoelectron spectroscopy (XPS) system designed for surface analysis. It provides precise and reliable data for the characterization of materials at the nanoscale level.
Sourced in United States
The Optima 8000 is an inductively coupled plasma optical emission spectrometer (ICP-OES) designed for elemental analysis. It provides high-performance, multi-element detection capabilities for a wide range of sample types. The instrument utilizes advanced optics and detector technology to deliver accurate and reliable results.
Sourced in Japan, United States, Germany, United Kingdom
The JEM-2100F is a transmission electron microscope (TEM) designed and manufactured by JEOL. It is capable of high-resolution imaging and analytical capabilities. The JEM-2100F is used for a variety of research and industrial applications that require advanced electron microscopy techniques.
Sourced in Germany, United States, United Kingdom, Netherlands, Spain, Japan, Canada, France, China, Australia, Italy, Switzerland, Sweden, Belgium, Denmark, India, Jamaica, Singapore, Poland, Lithuania, Brazil, New Zealand, Austria, Hong Kong, Portugal, Romania, Cameroon, Norway
The RNeasy Mini Kit is a laboratory equipment designed for the purification of total RNA from a variety of sample types, including animal cells, tissues, and other biological materials. The kit utilizes a silica-based membrane technology to selectively bind and isolate RNA molecules, allowing for efficient extraction and recovery of high-quality RNA.
More about "Spectrometry"
Spectrometry, also known as spectroscopy, is a powerful analytical technique that enables the identification and quantification of chemical compounds by measuring the interaction between matter and electromagnetic radiation.
This non-destructive method can be applied to a wide range of samples, from biological macromolecules to complex industrial mixtures.
Spectrometric techniques involve the separation of light into its constituent wavelengths, followed by the detection and analysis of the resulting spectrum.
These measurements provide valuable information about the chemical composition, structure, and properties of the analyte.
Spectrometry plays a crucial role in fields such as chemistry, physics, biology, and environmental science, facilitating advanced research, quality control, and diagnostic applications.
With continual advancements in instrumentation and data analysis, spectrometry remains an indispensable tool for scientists seeking to unveil the secrets of the physical world.
Spectrometers like the S-4800, Optima 8300, Optima 5300 DV, D8 Advance, and DU530 UV/VIS spectrophotometer are widely used in various applications, including the analysis of biological samples using reagents like TRIzol and the RNeasy Mini Kit.
Advanced spectrometric techniques, such as those employed by the ESCALAB 250Xi and Optima 8000, as well as electron microscopy instruments like the JEM-2100F, provide even deeper insights into the structure and properties of materials.
By leveraging the power of spectrometry, scientists can accelerate their research and drive breakthrough discoveries in diverse fields.
This non-destructive method can be applied to a wide range of samples, from biological macromolecules to complex industrial mixtures.
Spectrometric techniques involve the separation of light into its constituent wavelengths, followed by the detection and analysis of the resulting spectrum.
These measurements provide valuable information about the chemical composition, structure, and properties of the analyte.
Spectrometry plays a crucial role in fields such as chemistry, physics, biology, and environmental science, facilitating advanced research, quality control, and diagnostic applications.
With continual advancements in instrumentation and data analysis, spectrometry remains an indispensable tool for scientists seeking to unveil the secrets of the physical world.
Spectrometers like the S-4800, Optima 8300, Optima 5300 DV, D8 Advance, and DU530 UV/VIS spectrophotometer are widely used in various applications, including the analysis of biological samples using reagents like TRIzol and the RNeasy Mini Kit.
Advanced spectrometric techniques, such as those employed by the ESCALAB 250Xi and Optima 8000, as well as electron microscopy instruments like the JEM-2100F, provide even deeper insights into the structure and properties of materials.
By leveraging the power of spectrometry, scientists can accelerate their research and drive breakthrough discoveries in diverse fields.