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Merck

UPS1

Sigma-Aldrich

Universal Proteomics Standard Set

Protein Mass Spectrometry Calibration Standard

Sinonimo/i:

Standard Set

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Informazioni su questo articolo

Numero CE:
Codice UNSPSC:
12161503
NACRES:
NA.24
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Stato

ready-to-use solution

Livello qualitativo

Qualità

Protein Mass Spectrometry Calibration Standard

tecniche

mass spectrometry (MS): suitable

Temperatura di conservazione

−20°C

Categorie correlate

Descrizione generale

The Universal Proteomics Standard (UPS) Set was developed in collaboration with the Association of Biomolecular Resource Facilities (ABRF) Proteomics Standards Research Group (sPRG). This protein mixture was extensively evaluated and reported under the direction of ABRF′s sPRG during a comprehensive 2005/2006 study. The findings of the study were presented at the ABRF 2006 and US HUPO 2006 conferences.

Applicazioni

The Universal Proteomics Standard (UPS) Set is intended to standardize and/or evaluate mass spectrometric (e.g., LC-MS/MS, MALDI-TOF-MS, etc.) and electrophoretic analysis conditions prior to the analysis of complex protein samples. Potential uses include:
  • Bracketing critical experimental datasets for confirming the robustness of analysis methods
  • Comparison of MS or other proteomic data that are generated in different labs using a variety of analytical strategies and instruments
  • Identifying limitations of proteomics analysis systems and search algorithms
  • An external reference to assist with the evaluation of data derived from poorly defined samples

Caratteristiche e vantaggi

Discover the Benefits for Yourself!
  • Test the power of your analytical strategy
  • Troubleshoot and optimize your analytical protocol
  • Confirm system suitability before analyzing critical samples
  • Normalize analytical results day to day or lab to lab

I componenti del kit sono disponibili anche separatamente

N° Catalogo
Descrizione
SDS

  • T6567Trypsin from porcine pancreas, Proteomics Grade, BioReagent, Dimethylated 20 μgSDS

Avvertenze

Danger

Indicazioni di pericolo

Classi di pericolo

Acute Tox. 4 Oral - Eye Dam. 1 - Repr. 1B - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Organi bersaglio

Respiratory system

Codice della classe di stoccaggio

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

Classe di pericolosità dell'acqua (WGK)

WGK 3


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Leslie Muller et al.
Proteomics, 16(23), 2953-2961 (2016-10-18)
Sample preparation, typically by in-solution or in-gel approaches, has a strong influence on the accuracy and robustness of quantitative proteomics workflows. The major benefit of in-gel procedures is their compatibility with detergents (such as SDS) for protein solubilization. However, SDS-PAGE
Henrik Molina et al.
Analytical chemistry, 80(13), 4825-4835 (2008-06-11)
Electron transfer dissociation (ETD) is a recently introduced mass spectrometric technique which has proven to be an excellent tool for the elucidation of labile post-translational modifications such as phosphorylation and O-GlcNAcylation of serine and threonine residues. However, unlike collision induced
Mark V Ivanov et al.
Journal of proteome research, 13(4), 1911-1920 (2014-02-28)
Data-dependent tandem mass spectrometry (MS/MS) is one of the main techniques for protein identification in shotgun proteomics. In a typical LC-MS/MS workflow, peptide product ion mass spectra (MS/MS spectra) are compared with those derived theoretically from a protein sequence database.
Min-Sik Kim et al.
Journal of the American Society for Mass Spectrometry, 21(9), 1606-1611 (2010-05-21)
Shotgun proteomics has been used extensively for characterization of a number of proteomes. High-resolution Fourier transform mass spectrometry (FTMS) has emerged as a powerful tool owing to its high mass accuracy and resolving power. One of its major limitations, however
Chia-Yu Yen et al.
Molecular & cellular proteomics : MCP, 10(7), M111-M111 (2011-05-03)
The unambiguous assignment of tandem mass spectra (MS/MS) to peptide sequences remains a key unsolved problem in proteomics. Spectral library search strategies have emerged as a promising alternative for peptide identification, in which MS/MS spectra are directly compared against a

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