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Merck
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문서

MSP3H

Sigma-Aldrich

MS PhosphoMix 3 Heavy

Phosphopeptide Standard for MS

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About This Item

UNSPSC 코드:
12352200
NACRES:
NA.24

품질

Phosphopeptide Standard for MS

Quality Level

분석물 화학적 분류

amino acids, peptides, proteins

포장

pkg of 200 pmol total phosphopeptides

기술

HPLC: suitable
LC/MS: suitable

응용 분야

food and beverages

형식

multi-component solution

저장 온도

−20°C

일반 설명

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

법적 정보

This product is licensed under U.S. Patent No. 7,396,688 and foreign counterparts from E. I. du Pont de Nemours and Company. The purchase of this product conveys to the buyer the nontransferable right to use the purchased amount of the product for research and development only, including services for a third party for consideration. The buyer cannot sell or otherwise transfer this product, its components or materials made using this product or its components to a third party. Information about licenses for excluded uses is available from: E. I. du Pont de Nemours and Company; Attn: Associate Director, Commercial Development; DuPont Experimental Station E268; 200 Powdermill Rd.; Wilmington, DE 19803; 1-877-881-9787 (voice), 1-302-695-1437 (fax), licensing@dupont.com.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


시험 성적서(COA)

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문서 라이브러리 방문

Displacement of N/Q-rich peptides on TiO2 beads enhances the depth and coverage of yeast phosphoproteome analyses.
Kanshin, E., et al.
Journal of Proteome Research, 12(6), 1905-1913 (2013)
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
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
Jesper V Olsen et al.
Cell, 127(3), 635-648 (2006-11-04)
Cell signaling mechanisms often transmit information via posttranslational protein modifications, most importantly reversible protein phosphorylation. Here we develop and apply a general mass spectrometric technology for identification and quantitation of phosphorylation sites as a function of stimulus, time, and subcellular
Pieter Glibert et al.
Journal of proteome research, 14(2), 839-849 (2014-12-17)
The ability to distinguish between phosphopeptides of high and low stoichiometry is essential to discover the true extent of protein phosphorylation. We here extend the strategy whereby a peptide sample is briefly split in two identical parts and differentially labeled

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