Immerse yourself into the depths of the proteome

Going library-free for protein identification using Zeno SWATH DIA and in silico-generated spectral libraries

This Zeno SWATH DIA workflow, using an in silico-generated library processing with DIA-NN software, was superior to the traditional shotgun proteomics approach using Zeno DDA for the identification of large numbers of proteins from complex samples, and agreed with two commonly used experimentally generated libraries.

Zeno MS/MS with microflow chromatography powers the Zeno SWATH DIA workflow to quantify more proteins

As quantitative proteomics evolves, larger biological cohorts are being studied, often with precious samples. This creates the need to acquire data faster and with smaller amounts. Zeno SWATH DIA, with Zeno MS/MS and microflow LC, has the potential to significantly enhance core quantitative proteomics workflows.

High-throughput quantitative proteomics using Zeno SWATH DIA and the Evosep One system

Proteins and peptides are important in translational research to understand biological function. This method achieves 5-6x more MS/MS sensitivity, resulting in this DIA approach surpassing DDA for protein identifications and quantification in complex matrices.

Protein quantification at subnanogram loads using Zeno SWATH DIA and nanoflow chromatography

DIA has emerged as a comprehensive workflow for label-free quantitative proteomics, allowing for the acquisition of MS/MS spectra on all detectable peptides. Zeno SWATH DIA in the ZenoTOF 7600 system leverages Zeno trap activation for 5-6x increases in peptide MS/MS sensitivity in SWATH DIA workflows.

Large scale protein identification using microflow chromatography on the ZenoTOF 7600 system

Generation of spectral libraries is often thought of as a time consuming procedure, but in reality, they can be generated quickly. Using microflow chromatography with fast MS/MS acquisition on a QTOF, then searching the data in the cloud can enable library generation in <48 hrs.

Nanoflow Zeno SWATH DIA for high-sensitivity protein identification and quantification

Nanoflow chromatography is used in workflows to obtain the highest sensitivity. High-quality chromatographic separations are important, as good peak shape and peak resolution can reduce ion suppression and allow the MS system to sample as many unique peptides as possible.

Large-scale, targeted, peptide quantification of 804 peptides with high reproducibility, using Zeno MS/MS

A highly multiplex targeted peptide quantification assay has been developed to explore the quantitative capability of Zeno MS/MS. Using a mixture of 804 heavy labeled synthetic peptides dosed into plasma, the increase in peptide sensitivity due to Zeno MS/MS was found to be 5.6 fold.

PTM site localization and isomer differentiation of phosphorylated peptides

Specific location of phosphorylation sites on proteins is important in fully understanding their role in cellular processes. Here, the use and benefits of tunable electron activated dissociation (EAD) for phosphopeptide analysis and confident site-localization was evaluated on the ZenoTOF 7600 system.

Tunable electron activated dissociation (EAD) MS/MS to preserve particularly labile PTMs

Determining the identity and the precise location of a post-translational modification (PTM) on a protein is important to fully characterize function. Here, the utility of electron activated dissociation on the SCIEX ZenoTOF 7600 system was investigated for the characterization of labile PTMs.

Reproducible targeted peptide profiling using highly multiplexed MRM assays

Using the scheduled MRM algorithm to build highly multiplexed peptide MRM methods enables a higher number of MRMs to be monitored concurrently while maintaining optimal dwell and cycle times. The 7500 system for large scale targeted peptide quantification was evaluated using microflow chromatography.

Improved LC-MRM quantification sensitivity for cyclic peptides from the natriuretic peptide family

Cyclic peptides have been identified as important therapeutic modalities. This is related to their stability in blood and their potential for oral dosing. LC-MS method development to quantify trace levels of cyclic peptides in biological matrices has remained challenging.

Enhancing the sensitivity of peptide quantification for the targeted HCPs analysis

Host cell proteins (HCPs) are a major class of process-related impurities that accompany a recombinant biotherapeutic product during production. As their levels impact the potential toxicity and efficiency of the therapeutics, there are significant requirements for the quantitative measurement of HCPs across the entire development paradigm.