JPT's SpikeTidesTM Sets TAA are intelligent & low cost proteotypic peptide collections covering the 61 most important tumor associated antigens – TAA’s (Cheever et al., 2009).
- Identification & quantification of single & multiple TAAs by SRM/MRM
- Relative quantification of TAA expression levels
- Identification & optimization of assay conditions for proteotypic peptides
- Biomarker discovery and validation
- Clinical monitoring of therapeutic intervention and disease status
- Quantification of multiple TAA’s from a single sample
- First economic heavy labeled peptide set available
- Multiplexed analysis of disease status and therapeutic success
- ISO 9001:2008 Certification & GCLP Compliance
SpikeTidesTM Set TAA - light
252 unlabeled proteotypic peptides
--> only 225 USD
SpikeTidesTM Set TAA - heavy
252 isotopically labeled (13C & 15N) proteotypic peptides
--> only 450 USD
Synthesized to your specifications, incl. post-translational modifications
--> starting from 9 USD (light)
--> starting from 19 USD (heavy)
Testimonials for SpikeTidesTM
"My unit ... used JPT's various SpikeTides™ peptide products to build LC-MRM assays in a fast and cost efficient manner...."
Prof. Andrew Emili (CCBR, University of Toronto, Canada)
“We at the ETH successfully apply JPT’s unpurified isotope- and non-labeled peptide libraries for proteome-wide SRM assays allowing us to identify and quantify proteins spanning a broad range of abundances, including proteins not previously detectable...”
Paola Picotti, PhD (ISB, ETH Zürich, Switzerland)
"Occurrence and Detection of Phosphopeptide Isomers in Large-Scale Phosphoproteomics Experiments"
Courcelles et al., Journal of Proteome Research (2012)
"Using iRT, a Normalized Retention Time for more Targeted Measurement of Peptides"
Reiter et al., PROTEOMICS, Volume 12 (2012)
"Automated Workflow for Large-Scale Selected Reaction Monitoring Experiments"
Malmström et al., Journal of Proteome Research (2012)
"Peptides Quantification by Liquid Chromatography with Matrix-Assisted Laser Desorption/Ionization and Selected Reaction Monitoring Detection"
Lesur et al., Journal of Proteome Research (2012)
"Large-Scale Quantitative Assessment of Different In-Solution Protein Digestion Protocols Reveals Superior Cleavage Efficiency of Tandem Lys-C/Trypsin Proteolysis over Trypsin Digestion"
Glatter et al., Journal of Proteome Research (2012)
"Estimation of Absolute Protein Quantities of Unlabeled Samples by Selected Reaction Monitoring Mass Spectrometry"
Ludwig et al., Mol. Cell. Proteomics (2012)