Many biological questions are essentially spatial: why is a certain protein highly expressed only in the tumor region? Why does the modification state differ at the marginal band? Traditional proteomics homogenizes to measure average amounts, flattening these differences. Spatial proteomics uses MSI or spatial proteomics workflows to preserve structure, directly presenting the spatial heterogeneity of proteins/peptides.
In the Neo-Source product system, the MSI imaging sources (DPI, LDPI) provide in-situ acquisition capability of 'molecule–coordinate'; protein imaging can convert protein information into imageable peptide or ion signals via the appropriate sample preparation (e.g., enzymatic digestion, or matrix-assisted / matrix-free routes).
MSI can present in-situ the spatial distribution of polypeptides, protein-related ions and modification features; the Neo-Source MSI DPI is matrix-free, has low ion suppression and direct analysis of complex samples, with 20–200 μm adjustable resolution, suited to research that requires localizing protein-related signals within tissue.
Higher spatial-resolution needs (e.g., whether proteins localize to a certain cell band or subcellular structure) can be supplemented by the 2–3 μm matrix-free ambient imaging of the Neo-Source MSI LDPI, covering different scales from organ to single-cell/subcellular.
Protein imaging often requires preparation such as enzymatic digestion to convert proteins into measurable ions, combined with matrix or matrix-free routes. Results must be registered against validation methods such as immunofluorescence, IHC, and Western blot to confirm that the signal coincides with the expected histological structure. The two Neo-Source imaging sources keep the section intact after imaging for continued H&E or IHC validation.
The engineering value of matrix-free preparation is highlighted here: DPI and LDPI are matrix-free and measure on demand, reducing sample handling from 'at best half a day' down to on-demand measurement, significantly accelerating protein spatial research that requires many sample comparisons.
Protein MSI still faces challenges such as complex preparation, ionization-efficiency differences and quantitative calibration; conclusions should be cross-validated with complementary methods such as immunology, transcriptomics and metabolomics. Spatial proteomics is often combined with spatial metabolomics and spatial lipidomics to form multi-omics integrated imaging.
Engineered, the two Neo-Source imaging sources are compatible with mainstream mass spectrometers from Agilent, AB SCIEX and Thermo, providing a proprietary titanium-alloy ion-transfer tube that does not damage the sample at the front end and is detachable for cleaning, supporting stable and reproducible spatial proteomics research.
To obtain detailed specifications, compatible models, or a quotation for the MSI LDPI / DPI full series imaging ion sources, visit the Neo-Source official website, or contact the official team for compatibility advice tailored to your mass spectrometer (Agilent / SCIEX / Thermo and other mainstream MS).