226409-58-1

Basic information

• Product Name: (N-SUCCINIMIDYLOXYCARBONYLME.)TRIS(TRIME
• Synonyms: (N-SUCCINIMIDYLOXYCARBONYLME.)TRIS(TRIME;TMPP-Ac-OSu,N-Succinimidyl[tris(2,4,6-trimethoxyphenyl)phosphonio]acetateBromide;n-succinimidyl [tris(2,4,6-trimethoxyphenyl)phosphonio]acetate bromide;PhosphoniuM, [2-[(2,5-dioxo-1-pyrrolidinyl)oxy]-2-oxoethyl]tris(2,4,6-triMethoxyphenyl)-, broMide;TMPP-Ac-OSu;(N-Succinimidyloxycarbonylmethyl)tris(2,4,6-trimethoxyphenyl)phosphonium bromide, 96%, for protein sequence analysis (by MALDI-MS)
• CAS NO: 226409-58-1
• Molecular Formula: Br1C33H39N1O13P1
• Molecular Weight: 768.54
• Product Categories: Nitric Oxide Reagents;Cross Linking Reagents;MTS & Sulfhydryl Active Reagents
• Mol File: 226409-58-1.mol
• Article Data: 3

Chemical Properties

• Melting Point: 201-205 °C (dec.)
• Appearance: /
• Storage Temp.: −20°C
• Solubility: Chloroform (Slightly), Methanol (Slightly)
• CAS DataBase Reference: (N-SUCCINIMIDYLOXYCARBONYLME.)TRIS(TRIME(CAS DataBase Reference)
• NIST Chemistry Reference: (N-SUCCINIMIDYLOXYCARBONYLME.)TRIS(TRIME(226409-58-1)
• EPA Substance Registry System: (N-SUCCINIMIDYLOXYCARBONYLME.)TRIS(TRIME(226409-58-1)

Safety Data

• WGK Germany: 3
• F: 10-21
• Hazardous Substances Data: 226409-58-1(Hazardous Substances Data)

Usage

Description

(N-SUCCINIMIDYLOXYCARBONYLME.)TRIS(TRIME is a chemical compound that serves as a reagent for modifying the N-terminal of peptides. It is used in various applications, including fast atom bombardment (FAB) and matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS). (N-SUCCINIMIDYLOXYCARBONYLME.)TRIS(TRIME is an off-white solid and plays a crucial role in protein sequencing through MALDI MS.

Uses

Used in Mass Spectrometry:
(N-SUCCINIMIDYLOXYCARBONYLME.)TRIS(TRIME is used as a reagent for modifying the N-terminal of peptides in mass spectrometry applications. It aids in the analysis and identification of proteins by enhancing the ionization process during FAB or MALDI MS.
Used in Protein Sequencing:
In the field of protein sequencing, (N-SUCCINIMIDYLOXYCARBONYLME.)TRIS(TRIME is employed as a reagent for modifying the N-terminal of peptides. This modification is essential for accurate protein sequencing using MALDI MS, which is a widely used technique for determining the amino acid sequence of proteins.
Used in Pharmaceutical Industry:
(N-SUCCINIMIDYLOXYCARBONYLME.)TRIS(TRIME is used as a reagent in the pharmaceutical industry for protein analysis and characterization. Its role in protein sequencing and mass spectrometry helps researchers understand the structure and function of proteins, which is vital for drug discovery and development.
Used in Research and Development:
In research and development, (N-SUCCINIMIDYLOXYCARBONYLME.)TRIS(TRIME is utilized as a reagent for modifying the N-terminal of peptides. This modification is crucial for studying protein interactions, functions, and structures, which are essential for advancing scientific knowledge and developing new technologies in various fields, including biotechnology and biomedicine.

Upstream product

• 91608-15-0 tris(2,4,6-trimethoxyphenyl)phosphine 
• 42014-51-7 bromoacetic acid N-hydroxusuccinimidyl ester 

Relevant articles and documents

Coumarin tags for analysis of peptides by MALDI-TOF MS and MS/MS. 2. Alexa fluor 350 tag for increased peptide and protein identification by LC-MALDI-TOF/TOF MS

The goal of this study was the development of N-terminal tags to improve peptide identification using high-throughput MALDI-TOF/TOF MS. Part 1 of the study was focused on the influence of derivatization on the intensities of MALDI-TOF MS signals of peptides. In part 2, various derivatization approaches for the improvement of peptide fragmentation efficiency in MALDI-TOF/TOF MS are explored. We demonstrate that permanent cation tags, while significantly improving signal intensity in the MS mode, lead to severe suppression of MS/MS fragmentation, making these tags unsuitable for high-throughput MALDI-TOF/TOF MS analysis. In the present work, it was found that labeling with Alexa Fluor 350, a coumarin tag containing a sulfo group, along with guanidation of ε-amino groups of Lys, could enhance unimolecular fragmentation of peptides with the formation of a high-intensity y-ion series, while the peptide intensities in the MS mode were not severely affected. LC-MALDI-TOF/TOF MS analysis of tryptic peptides from the SCX fractions of an E. coli lysate revealed improved peptide scores, a doubling of the total number of peptides, and a 30% increase in the number of proteins identified, as a result of labeling. Furthermore, by combining the data from native and labeled samples, confidence in correct identification was increased, as many proteins were identified by different peptides in the native and labeled data sets. Additionally, derivatization was found not to impair chromatographic behavior of peptides. All these factors suggest that labeling with Alexa Fluor 350 is a promising approach to the high-throughput LC-MALDI-TOF/TOF MS analysis of proteomic samples.

Qualitative and quantitative analysis of small amine molecules by MALDI-TOF mass spectrometry through charge derivatization

A pair of isotopically coded light and heavy reagents, tris-(2,4,6- trimethoxyphenyl)phosphonium acetic acid-N-hydroxysuccinimide esters (1 and 2) were synthesized and used to derivatize low molecular weight (500 Da) molecules containing primary or secon