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UPS1

Sigma-Aldrich

Universal Proteomics Standard Set

Protein Mass Spectrometry Calibration Standard

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About This Item

EC Number:
232-650-8
UNSPSC Code:
12352200
NACRES:
NA.24

form

ready-to-use solution

Quality Level

200

quality

Protein Mass Spectrometry Calibration Standard

technique(s)

mass spectrometry (MS): suitable

storage temp.

−20°C

Related Categories

General description

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.

Application

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

Features and Benefits

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

Kit Components Also Available Separately

Product No.
Description
SDS
  • T6567Trypsin from porcine pancreas, Proteomics Grade, BioReagent, Dimethylated 20 μgSDS

Pictograms

Exclamation markHealth hazard
GHS07,GHS08

Signal Word

Danger

Hazard Statements

H315 - H319 - H334 - H335

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

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David L Tabb et al.
Journal of proteome research, 9(2), 761-776 (2009-11-20)
The complexity of proteomic instrumentation for LC-MS/MS introduces many possible sources of variability. Data-dependent sampling of peptides constitutes a stochastic element at the heart of discovery proteomics. Although this variation impacts the identification of peptides, proteomic identifications are far from
Stephane Houel et al.
Journal of proteome research, 9(8), 4152-4160 (2010-06-29)
A complicating factor for protein identification within complex mixtures by LC/MS/MS is the problem of "chimera" spectra, where two or more precursor ions with similar mass and retention time are co-sequenced by MS/MS. Chimera spectra show reduced scores due to
Matthew The et al.
Nature communications, 11(1), 3234-3234 (2020-06-28)
In shotgun proteomics, the analysis of label-free quantification experiments is typically limited by the identification rate and the noise level in the quantitative data. This generally causes a low sensitivity in differential expression analysis. Here, we propose a quantification-first approach
Christian J Koehler et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 25(1), 61-66 (2019-11-02)
Proteolytic digestion prior to LC-MS analysis is a key step for the identification of proteins. Digestion of proteins is typically performed with trypsin, but certain proteins or important protein sequence regions might be missed using this endoproteinase. Only few alternative
Amanda G Paulovich et al.
Molecular & cellular proteomics : MCP, 9(2), 242-254 (2009-10-28)
Optimal performance of LC-MS/MS platforms is critical to generating high quality proteomics data. Although individual laboratories have developed quality control samples, there is no widely available performance standard of biological complexity (and associated reference data sets) for benchmarking of platform
View All Related Papers

Articles

Universal Proteomics Standards – Validating the Future of Proteomics

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.

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UPS1 & UPS2 Proteomic Standards

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.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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