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UPS2

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Proteomics Dynamic Range 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

biological source

human

form

ready-to-use solution

quality

Protein Mass Spectrometry Calibration Standard

concentration

10.6 μg/ampule protein

technique(s)

mass spectrometry (MS): suitable

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

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.

Kit Components Also Available Separately

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

Signal Word

Danger

Hazard Classifications

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 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

高风险级别生物产品--人源产品

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Ozren Bogdanović et al.
Nature genetics, 48(4), 417-426 (2016-03-02)
The vertebrate body plan and organs are shaped during a conserved embryonic phase called the phylotypic stage. However, the mechanisms that guide the epigenome through this transition and their evolutionary conservation remain elusive. Here we report widespread DNA demethylation of
Lee Dicker et al.
Molecular & cellular proteomics : MCP, 9(12), 2704-2718 (2010-09-09)
Liquid chromatography-tandem mass spectrometry (LC-MS/MS)-based proteomics provides a wealth of information about proteins present in biological samples. In bottom-up LC-MS/MS-based proteomics, proteins are enzymatically digested into peptides prior to query by LC-MS/MS. Thus, the information directly available from the LC-MS/MS
PANDA: A comprehensive and flexible tool for quantitative proteomics data analysis
Chang C, et al.
Bioinformatics, 35, 898-900 (2018)
Christina Ludwig et al.
Molecular & cellular proteomics : MCP, 11(3), M111-M111 (2011-11-22)
For many research questions in modern molecular and systems biology, information about absolute protein quantities is imperative. This information includes, for example, kinetic modeling of processes, protein turnover determinations, stoichiometric investigations of protein complexes, or quantitative comparisons of different proteins
Minia Antelo-Varela et al.
Analytical chemistry, 91(18), 11972-11980 (2019-08-20)
The field of systems biology has been rapidly developing in the past decade. However, the data produced by "omics" approaches is lagging behind the requirements of this field, especially when it comes to absolute abundances of membrane proteins. In the
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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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