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UPS2

Sigma-Aldrich

Proteomics Dynamic Range Standard Set

Protein Mass Spectrometry Calibration Standard

Synonim(y):

Dynamic Range Standards, Proteomics Standard Set

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About This Item

Numer WE:
Kod UNSPSC:
12161503
NACRES:
NA.24

pochodzenie biologiczne

human

Poziom jakości

Postać

ready-to-use solution

jakość

Protein Mass Spectrometry Calibration Standard

stężenie

10.6 μg/ampule protein

metody

mass spectrometry (MS): suitable

Warunki transportu

wet ice

temp. przechowywania

−20°C

Opis ogólny

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.

Zastosowanie

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.
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Elementy zestawu są też dostępne oddzielnie

Numer produktu
Opis
Karta charakterystyki

  • T6567Trypsin from porcine pancreas, Proteomics Grade, BioReagent, Dimethylated 20 μgKarta charakterystyki

Hasło ostrzegawcze

Danger

Zwroty wskazujące rodzaj zagrożenia

Klasyfikacja zagrożeń

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

Organy docelowe

Respiratory system

Kod klasy składowania

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

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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
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
PANDA: A comprehensive and flexible tool for quantitative proteomics data analysis
Chang C, et al.
Bioinformatics, 35, 898-900 (2018)
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)
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

Produkty

High-throughput proteomics advances with improved analysis methods and mass spectrometry.

Powiązane treści

Standardize research with Universal and Dynamic Proteomics Standards, complex and well-characterized reference standards for mass spectrometry.

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