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UPS2

Sigma-Aldrich

Proteomics Dynamic Range Standard Set

Protein Mass Spectrometry Calibration Standard

Synonym(s):

Dynamic Range Standards, Proteomics Standard Set

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About This Item

EC Number:
232-650-8
UNSPSC Code:
12161503
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 Statements

H315,H318,H334,H335,H360F

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

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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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
Jacek R Wiśniewski et al.
Molecular systems biology, 8, 611-611 (2012-09-13)
We report a proteomic analysis of microdissected material from formalin-fixed and paraffin-embedded colorectal cancer, quantifying > 7500 proteins between patient matched normal mucosa, primary carcinoma, and nodal metastases. Expression levels of 1808 proteins changed significantly between normal and cancer tissues
Rosemary Yu et al.
Nature communications, 11(1), 1881-1881 (2020-04-22)
Cells maintain reserves in their metabolic and translational capacities as a strategy to quickly respond to changing environments. Here we quantify these reserves by stepwise reducing nitrogen availability in yeast steady-state chemostat cultures, imposing severe restrictions on total cellular protein and
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