Workflows and solutions
Collaborators across the proteomics ecosystem
Flexible workflow options, powered by SCIEX and supported by third-party collaborators across the proteomics ecosystem
Proteomics studies are only as strong as the full workflow, from separation and chromatography through acquisition and data processing. That’s why SCIEX works with third-party collaborators: to give researchers flexibility to build the right end-to-end workflow for their lab, while helping ensure the pieces work together for confident, reproducible results.
Evosep provides standardized, high‑throughput liquid chromatography for robust, reproducible proteomics workflows from discovery to large‑cohort studies.
SCIEX and Evosep integrate advanced LC and mass spectrometry, combining Evosep platforms—including Evosep Eno—with the ZenoTOF family and SCIEX 7500+ systems for fast, sensitive, and scalable LC‑MS.
IonOpticks develops high‑performance LC columns for proteomics, improving separation and reproducibility for confident LC‑MS results.
SCIEX and IonOpticks combine advanced chromatography with HRMS, pairing Aurora XS Series™ columns and HeatSync™ technologies with SCIEX ZenoTOF systems for stable, sensitive, and reproducible large‑scale proteomics.
PEAKS is an AI‑driven, de novo‑assisted platform developed by Bioinformatics Solutions Inc. (BSI) for comprehensive, confident LC‑MS/MS proteomics analysis.
As a supported collaborator, PEAKS processes high‑quality data from SCIEX ZenoTOF systems, converting Zeno trap–enabled acquisition (DDA, DIA, MRM) into high‑confidence IDs, reproducible quantitation, and streamlined, easy‑to‑validate workflows.
Developed and maintained by the MacCoss Lab at the University of Washington, Skyline is an open‑source platform for quantitative proteomics, supporting method development, data visualization, and assay quality assessment on complex LC‑MS data.
In collaboration with SCIEX, Skyline enables seamless processing and quantitative analysis of SCIEX data, delivering transparent, reproducible targeted proteomics workflows.
Proteomics FAQs
What is LC‑MS/MS proteomics, and why is LC–MS/MS the dominant technology?
Proteomics is the large-scale study of proteins, including their identification, quantitation, post-translational modifications (PTMs), and proteoforms across biological conditions. LC–MS/MS is the dominant technology because it combines high-resolution liquid chromatography with highly specific mass spectrometry and tandem MS detection. This enables deep coverage of complex samples while supporting both discovery and targeted quantitative workflows in a single analytical platform.
What is shotgun (bottom-up) proteomics?
Shotgun, or bottom-up, proteomics is a widely used approach where proteins are enzymatically digested into peptides prior to LC–MS/MS analysis. This strategy enables broad protein identification and quantitation across complex biological samples and supports the analysis of PTMs. Both data-dependent and data-independent acquisition methods are commonly used in shotgun proteomics workflows.
What is the difference between DDA (IDA) and DIA proteomics?
In data-dependent acquisition (DDA) or information-dependent acquisition (IDA), the mass spectrometer selects a subset of precursor ions for fragmentation in real time, which can maximize identifications but often leads to missing values across large sample sets. Data independent acquisition (DIA), including Zeno SWATH DIA and ZT Scan DIA, fragments all ions within defined m/z windows throughout the run. This creates a comprehensive and reproducible dataset that supports more consistent quantitation across cohorts, with data analysis playing a central role.
What problem does DIA or SWATH acquisition solve in proteomics?
DIA and SWATH acquisition address the issue of stochastic sampling and missing values commonly observed in DDA workflows. By systematically sampling the entire precursor space in every run, DIA enables more consistent peptide detection and quantitation across large sample sets, making it particularly well suited for translational, clinical, and systems biology studies.
What is targeted proteomics, and when should it be used?
Targeted proteomics focuses on a predefined list of peptides to achieve highly robust and reproducible quantitation. Multiple reaction monitoring (MRM) on triple quadrupole mass spectrometers is commonly used for verification, validation, and regulated studies. Targeted approaches are typically applied after discovery workflows to confirm and quantify proteins of interest across large numbers of samples.
Should I use a QTOF or a triple quadrupole for proteomics?
The choice depends on the measurement objective. QTOF systems are commonly used for discovery and broad profiling using DDA or DIA workflows, while triple quadrupole instruments are preferred for targeted quantitation using MRM when peptide targets are well defined. Many laboratories use both approaches, combining discovery-driven hypothesis generation with targeted verification and validation.
How do researchers balance depth, throughput, and robustness in proteomics?
Proteomics involves trade-offs between depth of coverage, sample throughput, and operational robustness. Nanoflow LC can maximize sensitivity and depth, while micro or analytical flow LC often improves robustness and reproducibility for high-throughput studies. Successful workflows typically prioritize stable, reproducible performance first, then optimize depth through method design, fractionation, or targeted follow-up rather than relying on a single parameter change.
How does SCIEX define proteomics performance beyond instrument sensitivity?
In practical proteomics, performance is determined by the entire analytical system, not just raw sensitivity. Chromatographic reproducibility, ionization stability, acquisition speed relative to chromatographic peak widths, and data processing strategy all contribute to meaningful results. SCIEX proteomics workflows are designed with this system-level perspective to support reproducible discovery and quantitative confidence across real-world studies.