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MSP1L

Sigma-Aldrich

MS PhosphoMix 1 Light

Phosphopeptide Standard for MS

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别名:
Phosphopeptide Standard for Mass Spectrometry
NACRES:
NA.24

质量

Phosphopeptide Standard for MS

质量水平

分析物化学类别

amino acids, peptides, proteins

包装

pkg of 200 pmol total phosphopeptides

technique(s)

HPLC: suitable
LC/MS: suitable

application(s)

food and beverages

格式

multi-component solution

储存温度

−20°C

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此商品
MSP3HMSRT1UPS2
Sigma-Aldrich

Sigma-Aldrich

MSP1L

MS PhosphoMix 1 Light

Sigma-Aldrich

Sigma-Aldrich

MSP3H

MS PhosphoMix 3 Heavy

Sigma-Aldrich

Sigma-Aldrich

MSRT1

MS RT 校准混合物

format

multi-component solution

format

multi-component solution

format

multi-component solution

format

-

quality

Phosphopeptide Standard for MS

quality

Phosphopeptide Standard for MS

quality

Proteomics Retention Time Standard for LC-MS

quality

Protein Mass Spectrometry Calibration Standard

analyte chemical class(es)

amino acids, peptides, proteins

analyte chemical class(es)

amino acids, peptides, proteins

analyte chemical class(es)

amino acids, peptides, proteins

analyte chemical class(es)

-

packaging

pkg of 200 pmol total phosphopeptides

packaging

pkg of 200 pmol total phosphopeptides

packaging

-

packaging

-

application(s)

food and beverages

application(s)

food and beverages

application(s)

food and beverages

application(s)

-

一般描述

The MS PhosphoMix line of products allows for the testing of the strengths and weaknesses of phosphopeptide sample processing, mass spectrometry analysis and instrument configurations. The mixes are produced from synthetic phosphopeptides with sequences derived from naturally occurring peptides as identified by Mann et al. in HeLa cells. Because the sequences are derived from mammalian cells, many natural phosphorylation motifs, such as those that present an abundance of proline, are represented. Additionally, the phosphopeptide distribution in each mix has been chosen to present a broad range of characteristics, including ionizability, LC retention time, charge state, and isoelectric point. Finally, PhosphoMix-1, 2, and 3 were designed in a complementary fashion, as highlighted on the following page. For example, all three mixes contain peptides of the same sequence with different sites of phosphorylation.

Each of the three phosphopeptides mixes are available in their naturally occurring isotopic abundances (light) or as stable isotope enriched versions (heavy), making the set of products highly amenable to quantitative analyses, allowing users to compare recovery between workflows or techniques.

  • Naturally occurring peptide sequences
  • Broad range of peptide characteristics
  • Complementary product designs
  • Available in light and heavy versions

More info and FASTA file

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

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Jordy J Hsiao et al.
Analytical chemistry, 90(15), 9457-9464 (2018-07-07)
Phosphorylated compounds and organic acids with multiple carboxylate groups are commonly observed to have poor peak shapes and signal in LC/MS experiments. The poor peak shape is caused by the presence of trace metals, particularly iron, contributed from a variety
Dorte B Bekker-Jensen et al.
Nature communications, 11(1), 787-787 (2020-02-09)
Quantitative phosphoproteomics has transformed investigations of cell signaling, but it remains challenging to scale the technology for high-throughput analyses. Here we report a rapid and reproducible approach to analyze hundreds of phosphoproteomes using data-independent acquisition (DIA) with an accurate site
Evgeny Kanshin et al.
Journal of proteome research, 12(6), 2905-2913 (2013-04-24)
Phosphorylation is a reversible protein modification that regulates major cellular processes such as cell division, growth, and differentiation through highly dynamic and complex signaling pathways. Large-scale phosphoproteomics analyses have been greatly facilitated using affinity chromatography such as metal oxide affinity
Daniel Schwartz et al.
Nature biotechnology, 23(11), 1391-1398 (2005-11-08)
With the recent exponential increase in protein phosphorylation sites identified by mass spectrometry, a unique opportunity has arisen to understand the motifs surrounding such sites. Here we present an algorithm designed to extract motifs from large data sets of naturally
Alexander R Ivanov et al.
Proteomics, 13(6), 904-909 (2013-01-16)
Proteomics is a rapidly transforming interdisciplinary field of research that embraces a diverse set of analytical approaches to tackle problems in fundamental and applied biology. This viewpoint article highlights the benefits of interlaboratory studies and standardization initiatives to enable investigators

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