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The MS PhosphoMix line of products allows for the testing of the strengths and weaknesses of phosphopeptide enrichment techniques, sample processing, and mass spectrometry based phosphoproteomics workflows. The products are also ideal reference materials to be used as “spike-ins” to gauge overall platform performance (e.g. recovery, sensitivity, repeatability) during routine phosphopeptide analysis. The MS PhosphoMix consists of mono-, di-, tri-, and tetra-phosphorylated synthetic peptides formulated into 3 uniquely designed mixtures (MS PhosphoMix 1, 2 and 3, see below). Each mixture is available in natural (light) and isotopically labeled (heavy) versions making the set of products highly amenable to quantitative analyses, allowing users to compare recovery between workflows or enrichment techniques. The complete set of 25 phosphopeptide sequences, containing a total of 46 phosphorylation sites on serine, threonine, and tyrosine residues are derived from human proteins, as identified by Mann et al. in HeLa cells.1 Many natural phosphorylation motifs, such as those that present an abundance of proline, are represented.2 Each of the three mixtures were designed to include phosphopeptides having a broad range of characteristics including peptide ionizability (both ESI and MALDI), molecular weight, chromatographic retention time, charge state, and isoelectric point. An additional design consideration and product highlight is the inclusion of complimentary peptides that have the same or similar amino acid sequence but in which the number of phosphorylated residues and/or site-specific location of phosphorylation vary.
MS PhosphoMix Product Concept
Ordering Information
Composition of PhosphoMix Products
Hover over image for larger view. Click here to open the image in a new window.
Hover over image for larger view. Click here to open the image in a new window. Complementary Peptide Series Hover over image for larger view. Click here to open the image in a new window. Hover over image for larger view. Click here to open the image in a new window. References
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