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Merck

MSP2L

MS PhosphoMix 2 Light

Phosphopeptide Standard for MS

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分類程式碼代碼:
12352200
NACRES:
NA.24

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品質

Phosphopeptide Standard for MS

品質等級

200

分析物化學類別

amino acids, peptides, proteins

包裝

pkg of 200 pmol total phosphopeptides

技術

HPLC: suitable
LC/MS: suitable

應用

food and beverages

形式

multi-component solution

儲存溫度

−20°C

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此商品
MSP1LMSP2HMSP1H
MS PhosphoMix 2 Light Phosphopeptide Standard for MS

Sigma-Aldrich

MSP2L

MS PhosphoMix 2 Light

MS PhosphoMix 1 Light Phosphopeptide Standard for MS

Sigma-Aldrich

MSP1L

MS PhosphoMix 1 Light

MS PhosphoMix 2 Heavy Phosphopeptide Standard for MS

Sigma-Aldrich

MSP2H

MS PhosphoMix 2 Heavy

MS PhosphoMix 1 Heavy Phosphopeptide Standard for MS

Sigma-Aldrich

MSP1H

MS PhosphoMix 1 Heavy

format

multi-component solution

format

multi-component solution

format

multi-component solution

format

multi-component solution

technique(s)

HPLC: suitable, LC/MS: suitable

technique(s)

HPLC: suitable, LC/MS: suitable

technique(s)

HPLC: suitable, LC/MS: suitable

technique(s)

HPLC: suitable, LC/MS: suitable

quality

Phosphopeptide Standard for MS

quality

Phosphopeptide Standard for MS

quality

Phosphopeptide Standard for MS

quality

Phosphopeptide Standard for MS

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)

amino acids, peptides, proteins

packaging

pkg of 200 pmol total phosphopeptides

packaging

pkg of 200 pmol total phosphopeptides

packaging

pkg of 200 pmol total phosphopeptides

packaging

pkg of 200 pmol total phosphopeptides

application(s)

food and beverages

application(s)

food and beverages

application(s)

food and beverages

application(s)

food and beverages

一般說明

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

儲存類別代碼

11 - Combustible Solids

水污染物質分類（WGK）

WGK 3

閃點（°F）

Not applicable

閃點（°C）

Not applicable

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number
SLCK4776
SLBR1632V
SLBF0168V
110M6078

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Isao Fukuda et al.
Journal of proteome research, 12(12), 5587-5597 (2013-11-20)
Metal oxide affinity chromatography (MOAC) represented by titanium dioxide (TiO2) chromatography has been used for phosphopeptide enrichment from cell lysate digests prior to mass spectrometry. For in-depth phosphoproteomic analysis, it is important for MOAC to achieve high phosphopeptide enrichment efficiency
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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