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Key Documents

UPS2

Sigma-Aldrich

Proteomics Dynamic Range Standard Set

Protein Mass Spectrometry Calibration Standard

Synonyme(s) :

Dynamic Range Standards, Proteomics Standard Set

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About This Item

Numéro CE :
Code UNSPSC :
12161503
Nomenclature NACRES :
NA.24

Source biologique

human

Forme

ready-to-use solution

Qualité

Protein Mass Spectrometry Calibration Standard

Concentration

10.6 μg/ampule protein

Technique(s)

mass spectrometry (MS): suitable

Conditions d'expédition

wet ice

Température de stockage

−20°C

Description générale

The Proteomics Dynamic Range Standard Set is produced from a mixture of 48 individual human source or human sequence recombinant proteins, each of which has been selected to limit heterogeneous post-translational modifications (PTMs). The protein standard is formulated from 6 mixtures of 8 proteins to present a dynamic range of 5 orders of magnitude, ranging from 50 pmoles to 500 amoles. Each protein has been quantitated by amino acid analysis (AAA) prior to formulation.

Application

Proteomics Dynamic Range Standard Set has been used in the intensity-based absolute quantification (iBAQ) of E .coli proteins, embryonic stem cells (ESCs) and neuronal precursor cells (NPCs) proteomes. It has also been used as a standard to spike HeLa cells for label-free quantification.
The Proteomics Dynamic Range Standard Set can be used 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. UPS2 can be used to bracket precious experimental data sets between runs of a known complex standard sample. This allows confirmation of the robustness of the analysis method and stability of the instrument employed. Additionally, laboratories generating or comparing mass spectrometric data derived from poorly defined samples can use UPS2 as an external reference to assist with the evaluation of results and experimental methodology.
Proteomics Dynamic Range Standard Set has been used for the quantification of dynamic range universal protein standard on Orbitrap Analyzer using all ion fragmentation. It has been used as a standard for intensity-based absolute quantification of proteins (iBAQ) in LC-MS (liquid chromatography-mass spectrometry)/MS analysis.

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Réf. du produit
Description
FDS

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

Pictogrammes

Health hazardCorrosionExclamation mark

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

Eye Dam. 1 - Repr. 1B - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Organes cibles

Respiratory system

Code de la classe de stockage

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

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Boumediene Soufi et al.
Frontiers in microbiology, 6, 103-103 (2015-03-06)
We set out to provide a resource to the microbiology community especially with respect to systems biology based endeavors. To this end, we generated a comprehensive dataset monitoring the changes in protein expression, copy number, and post translational modifications in
Erik Ahrné et al.
Proteomics, 13(17), 2567-2578 (2013-06-25)
There is a great interest in reliable ways to obtain absolute protein abundances at a proteome-wide scale. To this end, label-free LC-MS/MS quantification methods have been proposed where all identified proteins are assigned an estimated abundance. Several variants of this
An interaction landscape of ubiquitin signaling
Zhang X, et al.
Molecular Cell, 65(5), 941-955 (2017)
L Arike et al.
Journal of proteomics, 75(17), 5437-5448 (2012-07-10)
Three different label-free proteome quantification methods--APEX, emPAI and iBAQ--were evaluated to measure proteome-wide protein concentrations in the cell. All the methods were applied to a sample from Escherichia coli chemostat culture. A Pearson squared correlation of approximately 0.6 among the
Jürgen Cox et al.
Molecular & cellular proteomics : MCP, 13(9), 2513-2526 (2014-06-20)
Protein quantification without isotopic labels has been a long-standing interest in the proteomics field. However, accurate and robust proteome-wide quantification with label-free approaches remains a challenge. We developed a new intensity determination and normalization procedure called MaxLFQ that is fully

Articles

High-throughput proteomics advances with improved analysis methods and mass spectrometry.

High-throughput proteomics advances with improved analysis methods and mass spectrometry.

High-throughput proteomics advances with improved analysis methods and mass spectrometry.

High-throughput proteomics advances with improved analysis methods and mass spectrometry.

Contenu apparenté

Standardize research with Universal and Dynamic Proteomics Standards, complex and well-characterized reference standards for mass spectrometry.

Standardize research with Universal and Dynamic Proteomics Standards, complex and well-characterized reference standards for mass spectrometry.

Standardize research with Universal and Dynamic Proteomics Standards, complex and well-characterized reference standards for mass spectrometry.

Standardize research with Universal and Dynamic Proteomics Standards, complex and well-characterized reference standards for mass spectrometry.

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