UPS2

Sigma-Aldrich

Proteomics Dynamic Range Standard Set

Protein Mass Spectrometry Calibration Standard

EC Number:
NACRES:
NA.24

Quality Level

quality

Protein Mass Spectrometry Calibration Standard

concentration

10.6 μg/ampule protein

shipped in

wet ice

storage temp.

−20°C

Related Categories

General description

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

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.
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.

Kit Components Also Available Separately

Product No.
Description
SDS

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

Pictograms

Exclamation markHealth hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Target Organs

Respiratory system

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
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)
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...
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...
Taejoon Kwon et al.
Journal of proteome research, 10(7), 2949-2958 (2011-04-15)
Shotgun proteomics using mass spectrometry is a powerful method for protein identification but suffers limited sensitivity in complex samples. Integrating peptide identifications from multiple database search engines is a promising strategy to increase the number of peptide identifications and reduce...
Articles
The era of high-throughput proteomics has recently blossomed due in large part to advances in the methods by which proteins and proteomes are analyzed. Improved fractionation techniques, combined with advances in mass spectrometry, have decreased concerns of sample complexity, and directed more focus towards high-throughput techniques.
Read More
Related Content
Standardize Your Research. We offer both the Universal Proteomics Standard and the Proteomics Dynamic range Standard as complex, well-defined, well characterized reference standards for mass spectrometry.
Read More

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