Generate comprehensive, quantitative proteome maps to address complex biological questions. Our discovery workflows support unbiased analysis across a wide range of sample types and applications, combining label-free DIA with robust, optimized protein preparation for consistent and high-quality data.
Biognosys Discovery Proteomics provides unbiased proteome profiling for a broad range of applications and sample types.
Our end‑to‑end services integrate optimized sample preparation, high performance DIA LC–MS acquisition methods, and advanced data analysis. We deliver deep proteome coverage from low input amounts across tissues, cell lines, and biofluids, with consistent and reproducible quantification.
Our Discovery Proteomics covers experimental designs from small studies to large cohorts.
Industry-leading proteome coverage delivering up to 13,000 quantified proteins from human cell lines or tissues and up to 9,000 proteins from plasma samples.
Automated and reproducible sample preparation with stringent quality controls, providing median protein-level CVs below 10% and near-zero batch effects, even across large cohorts.
Screening-compatible throughput options enabling the generation of hundreds of high-quality proteomes per day, supporting large scale discovery and cohort-based studies.
Expert data interpretation, advanced statistical analysis, and result consolidation in close exchange with our customers, delivered by dedicated project managers.
1. Sample Input Format –Universal Compatibility
Reliable proteome quantification across diverse biospecimens with high performance at low input amounts.
2. Protein Enrichment (optional)
Protein corona-based enrichment for biofluids enhances detection of low-abundance protein biomarkers. Not required for cells and tissue samples.
3. Digestion – Protein Extraction
Automated, high-throughput sample preparation enabling efficient protein extraction while maintaining the original proteome composition.
4. LCMS – High-Throughput DIA-based Quantification
LC-MS/MS-based proteome profiling using standardized, highly optimized acquisition routines on state-of-the-art mass spectrometers.
5. Data Analysis / Interpretation – Actionable Proteomic Insights
Combination of AI-powered Spectronaut analytics with dedicated project management to transform discovery proteomics data into actionable biological insights.
Proteomics Service
Biognosys Tissue Proteomics enables biomarker discovery, target validation, and mechanism‑of‑action studies with fresh frozen and FFPE tissue samples.
From as little as 1 mg of fresh frozen tissue or a single FFPE slide, we provide deep proteome coverage that includes intracellular, membrane-bound, secreted, and extracellular proteins. With this depth Tissue Proteomics covers therapeutically relevant targets in e.g. translational studies and clinical research.
The platform is based on label‑free, quantitative DIA mass spectrometry combined with optimized sample preparation and stringent quality control. Advanced data analysis using Biognosys’ Spectronaut software, ensures high data completeness, precise quantification, and scalable tissue proteomics.
Proteomics Service
Biognosys Plasma Proteomics enables large-scale, unbiased biomarker discovery and translational research directly in blood plasma. By addressing the wide dynamic range of plasma proteins, the approach supports the confident identification of low-abundance, disease-relevant proteins, making it well suited for discovery studies and cohort-level analyses.
We deliver deep and reproducible plasma proteome profiling with comprehensive coverage of signaling proteins, cytokines, growth factors, and other low-abundance biomarkers. Our data provides the quantitative consistency required for large cohorts and longitudinal studies across translational and clinical research settings.
The workflow is powered by Biognosys’ proprietary P2 Plasma Enrichment technology, which uses nanoparticle-based protein enrichment to cover a wider dynamic range and enhance detection of low-abundance proteins with label-free DIA mass spectrometry.
Proteomics Service
Biognosys CSF Proteomics enables unbiased biomarker discovery and biological insight into central nervous system (CNS) disorders. Cerebrospinal fluid is in direct contact with the brain and spinal cord and therefore reflects CNS pathology more directly than peripheral biofluids. Proteomic analysis of CSF supports the identification of disease-related processes, early pathological changes, and pharmacodynamic responses in neurodegenerative and neuroinflammatory diseases.
Using advanced enrichment strategies, we deliver in-depth CSF proteome profiling with coverage of up to ~6,000 proteins, including low-abundance and CNS-specific proteins. This depth enables the detection of biomarkers related to neuronal function, synaptic biology, neuroinflammation, and myelination, supporting discovery and translational studies in indications such as Alzheimer’s disease, Parkinson’s disease, multiple sclerosis, and other CNS disorders.
CSF profiling is based on optimized protein enrichment combined with label-free, DIA mass spectrometry to address the limited protein content and dynamic range of CSF samples. Standardized sample preparation, high-performance LC–MS acquisition, and advanced data analysis using Spectronaut ensure high data completeness and reproducible quantification.
Proteomics Service
Biognosys Glycoproteomics enables systematic profiling of the cell surfaceome to support biomarker discovery, target identification, and therapeutic development. Cell surface proteins play a central role in cell–cell communication, signal transduction, and immune recognition and are among the most druggable classes of proteins.
Our N-glycoproteomics workflows provide comprehensive and selective coverage of N-glycosylated surface proteins, enabling confident identification of receptors, transporters, adhesion molecules, and immune-related targets. The approach enriches low-abundance surface proteins that are often masked in bulk proteome analysis, supporting comparative surfaceome profiling across cell lines, treatments, or genetic perturbations.
Surfaceome profiling is implemented through N-glycopeptide enrichment integrated into our label-free DIA proteomics platform.
Proteomics Service
Biognosys Cell Line Proteomics enables large-scale, unbiased proteomic screening to support functional biology, drug discovery, and mechanism-of-action studies.
We provide proteome-wide profiling of human and non-human cell lines using workflows optimized for screening applications. Per cell line, we routinely quantify up to ~10,000 proteins with high reproducibility, enabling robust comparisons across hundreds to thousands of samples and supporting studies that capture biological variability across treatments, genotypes, or perturbations.
Cell line profiling is based on standardized sample preparation combined with label-free, DIA mass spectrometry. High-throughput acquisition strategies and advanced data analysis using Spectronaut ensure reproducible, scalable proteomics, with expert project management supporting reliable interpretation in screening and discovery studies.
Proteomics Service
Biognosys Phosphoproteomics enables the systematic analysis of cellular signaling networks to support oncology research, early drug discovery, and mechanism-of-action studies. By directly measuring phosphorylation events at scale, it provides insight into pathway activation, kinase signaling, and treatment response that cannot be reliably inferred from transcriptomic or total proteome data alone.
From cell pellets or fresh frozen tissue, we routinely quantify ~25,000–65,000 class I phosphopeptides per study. This depth enables comprehensive coverage of key signaling pathways, supporting the identification of regulated phosphorylation sites, pathway-level changes, and phosphorylation targets for downstream validation across a range of experimental designs.
The workflow combines phosphopeptide enrichment with label-free DIA mass spectrometry. Data analysis is performed using Spectronaut with dedicated PTM workflows, enabling confident site identification, accurate quantification, and reproducible phosphoproteomic profiling across studies.
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