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UPS2

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Proteomics Dynamic Range Standard Set

Protein Mass Spectrometry Calibration Standard

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EC Number:
NACRES:
NA.24

biological source

human

Quality Level

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

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UPS1EMS0004EMS0005
Universal Proteomics Standard Set Protein Mass Spectrometry Calibration Standard

UPS1

Universal Proteomics Standard Set

SOLu-Trypsin recombinant, expressed in Pichia pastoris, Proteomics Grade, liquid

EMS0004

SOLu-Trypsin

Sigma-Aldrich

EMS0005

SOLu-Trypsin Dimethylated

technique(s)

mass spectrometry (MS): suitable

technique(s)

mass spectrometry (MS): suitable

technique(s)

-

technique(s)

-

concentration

10.6 μg/ampule protein

concentration

-

concentration

-

concentration

-

form

ready-to-use solution

form

ready-to-use solution

form

ready-to-use solution

form

ready-to-use solution

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

shipped in

wet ice

shipped in

-

shipped in

wet ice

shipped in

wet ice

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

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

6.1C - Combustible, acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
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
Absolute proteome and phosphoproteome dynamics during the cell cycle of Schizosaccharomyces pombe (Fission Yeast).
Carpy A, et al.
Molecular and Cellular Proteomics, 13, 1925-1925 (2014)
PANDA: A comprehensive and flexible tool for quantitative proteomics data analysis
Chang C, et al.
Bioinformatics, 35, 898-900 (2018)
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

Articles

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.

Related Content

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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