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UPS1

Sigma-Aldrich

Universal Proteomics Standard Set

Protein Mass Spectrometry Calibration Standard

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Synonym(s):
Universal Proteomics Standard for Mass Spectrometry
EC Number:
232-650-8
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

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

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T1503
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25G
Pack Size/Quantity

Additional examples:

705578-5MG-PW

PL860-CGA/SHF-1EA

MMYOMAG-74K-13

1000309185

enter as 1.000309185)

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Lot and Batch Numbers can be found on a product's label following the words 'Lot' or 'Batch'.

Aldrich Products

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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.
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
Markus Brosch et al.
Molecular & cellular proteomics : MCP, 7(5), 962-970 (2008-01-25)
It is a major challenge to develop effective sequence database search algorithms to translate molecular weight and fragment mass information obtained from tandem mass spectrometry into high quality peptide and protein assignments. We investigated the peptide identification performance of Mascot
W Sean Davidson et al.
Arteriosclerosis, thrombosis, and vascular biology, 29(6), 870-876 (2009-03-28)
Recent proteomic studies have identified multiple proteins that coisolate with human HDL. We hypothesized that distinct clusters of protein components may distinguish between physicochemically-defined subpopulations of HDL particles, and that such clusters may exert specific biological function(s). We investigated the
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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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