form
ready-to-use solution
Quality Level
quality
Protein Mass Spectrometry Calibration Standard
technique(s)
mass spectrometry (MS): suitable
storage temp.
−20°C
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 μg
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Acute Tox. 4 Oral - Eye Dam. 1 - Repr. 1B - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
WGK
WGK 3
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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
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
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
Antonio Palomba et al.
Journal of proteome research, 20(7), 3497-3507 (2021-05-27)
MS1-based label-free quantification can compare precursor ion peaks across runs, allowing reproducible protein measurements. Among bioinformatic platforms enabling MS1-based quantification, MaxQuant (MQ) is one of the most used, while Proteome Discoverer (PD) has recently introduced the Minora tool. Here, we
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
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