TCI America Girard's Reagent T B0457

Description
Girard's Reagent T / (Hydrazinocarbonylme thyl)trimethylammoni um Chloride Mass spectrometry (MS) is the method for determining the mass-to-charge ratio (m/z) of a molecule or an atom and obtaining information such as a molecular weight. To determine m/z, first it is necessary to ionize target analytes. Electron impact (EI) is known as the easiest ionization method. However, the mass spectrum obtained by EI is complicated because of easy fragmentation which sometimes makes it hard to analyze. So softer ionization methods which cause less fragmentation have been developed. They include fast atom bombardment ionization (FAB), electron spray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI). These softer ionization methods can provide high-quality spectra without unnecessary fragmentation. One of the main reasons of today's successful proteome analysis is the development of the mass spectrometry technique using soft ionization methods. The speed of protein analysis has been significantly improved for the two following reasons; 1) establishment of the soft ionization method of proteins using ESI and MALDI, 2) enhancement of precision, sensitivity and speed of time-of-flight mass spectrometry (TOF-MS). In 1993, the peptide mass fingerprinting (PMF) method was developed, which enabled rapid proteome analysis. Now, MS is used as an important analytical tool not only in the field of chemistry but also in the field of biological science. MS is also used for the analysis of trace amounts of biologically active small molecules in living bodies. For analysis of biologically active small molecules in a complicated biological matrix, LC-MS is commonly used. In these cases the sample is separated by HPLC and the quantity is determined by MS. FAB and ESI are used as ionization methods for LC-MS, in which vaporization of the sample is not required. Especially, ESI is the most used ionization method for LC-MS because it causes less fragmentation and has a wide range of applicable compounds and high operability. However, in today's advanced research, sometimes we can not get sufficient detection for trace amounts of components even using highly-sensitive LC-ESI-MS. In that case, derivatization reagents for MS are used to increase detection sensitivity for ESI-MS. The derivatization reagents have functional groups in the molecule that stabilize positive or negative charge.
Description
Girard's Reagent T / (Hydrazinocarbonylme thyl)trimethylammoni um Chloride Mass spectrometry (MS) is the method for determining the mass-to-charge ratio (m/z) of a molecule or an atom and obtaining information such as a molecular weight. To determine m/z, first it is necessary to ionize target analytes. Electron impact (EI) is known as the easiest ionization method. However, the mass spectrum obtained by EI is complicated because of easy fragmentation which sometimes makes it hard to analyze. So softer ionization methods which cause less fragmentation have been developed. They include fast atom bombardment ionization (FAB), electron spray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI). These softer ionization methods can provide high-quality spectra without unnecessary fragmentation. One of the main reasons of today's successful proteome analysis is the development of the mass spectrometry technique using soft ionization methods. The speed of protein analysis has been significantly improved for the two following reasons; 1) establishment of the soft ionization method of proteins using ESI and MALDI, 2) enhancement of precision, sensitivity and speed of time-of-flight mass spectrometry (TOF-MS). In 1993, the peptide mass fingerprinting (PMF) method was developed, which enabled rapid proteome analysis. Now, MS is used as an important analytical tool not only in the field of chemistry but also in the field of biological science. MS is also used for the analysis of trace amounts of biologically active small molecules in living bodies. For analysis of biologically active small molecules in a complicated biological matrix, LC-MS is commonly used. In these cases the sample is separated by HPLC and the quantity is determined by MS. FAB and ESI are used as ionization methods for LC-MS, in which vaporization of the sample is not required. Especially, ESI is the most used ionization method for LC-MS because it causes less fragmentation and has a wide range of applicable compounds and high operability. However, in today's advanced research, sometimes we can not get sufficient detection for trace amounts of components even using highly-sensitive LC-ESI-MS. In that case, derivatization reagents for MS are used to increase detection sensitivity for ESI-MS. The derivatization reagents have functional groups in the molecule that stabilize positive or negative charge.

Suppliers

Company
Product
Description
Supplier Links
Girard's Reagent T - B0457 - TCI America
Portland, OR, USA
Girard's Reagent T
B0457
Girard's Reagent T B0457
Girard's Reagent T / (Hydrazinocarbonylme thyl)trimethylammoni um Chloride Mass spectrometry (MS) is the method for determining the mass-to-charge ratio (m/z) of a molecule or an atom and obtaining information such as a molecular weight. To determine m/z, first it is necessary to ionize target analytes. Electron impact (EI) is known as the easiest ionization method. However, the mass spectrum obtained by EI is complicated because of easy fragmentation which sometimes makes it hard to analyze. So softer ionization methods which cause less fragmentation have been developed. They include fast atom bombardment ionization (FAB), electron spray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI). These softer ionization methods can provide high-quality spectra without unnecessary fragmentation. One of the main reasons of today's successful proteome analysis is the development of the mass spectrometry technique using soft ionization methods. The speed of protein analysis has been significantly improved for the two following reasons; 1) establishment of the soft ionization method of proteins using ESI and MALDI, 2) enhancement of precision, sensitivity and speed of time-of-flight mass spectrometry (TOF-MS). In 1993, the peptide mass fingerprinting (PMF) method was developed, which enabled rapid proteome analysis. Now, MS is used as an important analytical tool not only in the field of chemistry but also in the field of biological science. MS is also used for the analysis of trace amounts of biologically active small molecules in living bodies. For analysis of biologically active small molecules in a complicated biological matrix, LC-MS is commonly used. In these cases the sample is separated by HPLC and the quantity is determined by MS. FAB and ESI are used as ionization methods for LC-MS, in which vaporization of the sample is not required. Especially, ESI is the most used ionization method for LC-MS because it causes less fragmentation and has a wide range of applicable compounds and high operability. However, in today's advanced research, sometimes we can not get sufficient detection for trace amounts of components even using highly-sensitive LC-ESI-MS. In that case, derivatization reagents for MS are used to increase detection sensitivity for ESI-MS. The derivatization reagents have functional groups in the molecule that stabilize positive or negative charge.

Girard's Reagent T / (Hydrazinocarbonylmethyl)trimethylammonium Chloride
Mass spectrometry (MS) is the method for determining the mass-to-charge ratio (m/z) of a molecule or an atom and obtaining information such as a molecular weight. To determine m/z, first it is necessary to ionize target analytes. Electron impact (EI) is known as the easiest ionization method. However, the mass spectrum obtained by EI is complicated because of easy fragmentation which sometimes makes it hard to analyze. So softer ionization methods which cause less fragmentation have been developed. They include fast atom bombardment ionization (FAB), electron spray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI). These softer ionization methods can provide high-quality spectra without unnecessary fragmentation.
One of the main reasons of today's successful proteome analysis is the development of the mass spectrometry technique using soft ionization methods. The speed of protein analysis has been significantly improved for the two following reasons; 1) establishment of the soft ionization method of proteins using ESI and MALDI, 2) enhancement of precision, sensitivity and speed of time-of-flight mass spectrometry (TOF-MS). In 1993, the peptide mass fingerprinting (PMF) method was developed, which enabled rapid proteome analysis. Now, MS is used as an important analytical tool not only in the field of chemistry but also in the field of biological science.
MS is also used for the analysis of trace amounts of biologically active small molecules in living bodies. For analysis of biologically active small molecules in a complicated biological matrix, LC-MS is commonly used. In these cases the sample is separated by HPLC and the quantity is determined by MS. FAB and ESI are used as ionization methods for LC-MS, in which vaporization of the sample is not required. Especially, ESI is the most used ionization method for LC-MS because it causes less fragmentation and has a wide range of applicable compounds and high operability. However, in today's advanced research, sometimes we can not get sufficient detection for trace amounts of components even using highly-sensitive LC-ESI-MS. In that case, derivatization reagents for MS are used to increase detection sensitivity for ESI-MS. The derivatization reagents have functional groups in the molecule that stabilize positive or negative charge.

Supplier's Site

Technical Specifications

  TCI America
Product Category Chemical Additives and Agents
Product Number B0457
Product Name Girard's Reagent T
Unlock Full Specs
to access all available technical data

Similar Products

Polyaphaolefin (PAO) Base Stock - SpectraSyn Plus™ 3.6 - ExxonMobil Chemical Company - Synthetic Base Stocks
ExxonMobil Chemical Company - Synthetic Base Stocks
Specs
Applications Oils & Fuels
Form & Features Liquids
View Details
Exfola™ - Surface Modifier - Mitsui Chemicals America, Inc.
Mitsui Chemicals America, Inc.
Specs
Function Unlisted, Proprietary or Specialized Function; Surface Modifier
Applications Packaging
View Details
Buffered Carbonate Solution - pH10 -  - Myron L Company
Specs
Function Buffer / Buffering Agent
Form & Features Liquids
View Details
Light-Curable Materials, Activators, 535-A-REV-A -  - Dymax
Specs
Applications Adhesives or Sealants
View Details