Acetyl-Proteomics Services
Acetyl-Proteomics Services
What Is Acetylation and Why Is It Important?
MetwareBio's Acetylation Proteomics Service utilizes advanced 4D label-free LC-MS/MS technology to provide high-resolution, quantitative profiling of protein acetylation events. Our workflow enables precise identification and site-specific quantification of acetylated peptides, offering researchers deep insights into acetylation-mediated regulatory mechanisms and protein interaction networks. This service is well-suited for applications such as mechanistic studies, targeted pathway analysis, epigenetic research, and biomarker discovery, supporting diverse fields including oncology, cell signaling, and epigenetics.
N-terminal and lysine protein acetylation (Ree et al., 2018)
Why Choose MetwareBio for Acetylation Analysis?
Acetylation Proteomics Workflow Using LC-MS/MS
Enrichment
Detection
Acetyl-Proteomics Service Deliverables
Applications of Acetylation Analysis in Research
Protein acetylation, particularly lysine acetylation, plays a key role in gene regulation, epigenetic modification, and cellular metabolism, making it highly relevant to disease mechanisms. Abnormal acetylation patterns are frequently observed in cancer, neurodegenerative diseases, and metabolic disorders. Acetylation proteomics enables researchers to explore changes in histone and non-histone acetylation under pathological conditions, supporting the identification of biomarkers, therapeutic targets, and epigenetic regulators in clinical research and drug development.
In model organisms such as mice, zebrafish, and Drosophila, lysine acetylation regulates a wide range of physiological processes, including development, immune response, and metabolic homeostasis. Acetylation profiling in animal models allows researchers to dissect post-translational regulation in vivo, assess disease progression, and evaluate the effect of therapeutic interventions. It also supports the discovery of acetylation-dependent pathways involved in aging, tissue regeneration, and signal transduction.
In plants, acetylation modulates chromatin remodeling, gene expression, and photosynthetic regulation. It also plays a crucial role in mediating responses to environmental stressors such as drought, salinity, and pathogen attack. Acetylation proteomics helps uncover the functional roles of histone and non-histone acetylation in developmental control, hormone signaling, and stress adaptation, contributing to crop improvement and resilience research.
In bacteria and fungi, acetylation regulates enzyme activity, metabolic pathways, and antibiotic resistance. In host–microbe interactions, both microbial and host protein acetylation can be dynamically modulated, influencing infection outcomes. Acetylation profiling in microbial systems or environmental samples reveals key mechanisms of stress tolerance, virulence regulation, and adaptation to complex habitats, supporting research in microbiology, biotechnology, and environmental science.
Sample Requirements for Acetylation Analysis
We support a wide range of sample types. Refer to the recommended amounts below:
| Category | Sample Type | Recommended Sample Size | Minimum Sample Size |
| Animal Tissue | Normal Tissues, Red Bone Marrow, Soft-bodied Insects | 100mg | 50mg |
| Chitinous Insects | 2 g | 1g | |
| Yellow Bone Marrow | 200mg | 100mg | |
| Plant Tissue | Young Leaves, Petals, Callus) | 1g | 500mg |
| Mature leaves, Stems, Algae, Macrofungi | 2g | 1g | |
| Bark, Roots, and Fruits | 5g | 3g | |
| Bioliquid | Amniotic Fluid, milk | 600μL | 300μL |
| Cell | Primary Cells | 2×10^7 | \ |
| Sperm, Platelets | 4×10^8 | 2×10^8 | |
| Passaged Cells | 2×10^7 | \ | |
| Microorganism | Bacteria | 500mg | 200mg |
| Fungi | 1g | 500mg | |
| Protein | Protein Solution | 5mg | 3mg |
- At least 3 biological replicates are recommended. For animal models, 3–6 subjects are suggested; for clinical samples, 6–10 cases are advised.
- Please refer to our Sample Preparation Handbook and Sample Submission Guidelines for detailed instructions, or contact us for customized support.
FAQ on Acetyl-proteomics and Acetylation Analysis
Lysine acetylation is a reversible post-translational modification where an acetyl group is covalently added to the ε-amino group of lysine residues. It plays a central role in regulating protein function, stability, subcellular localization, and interactions. Acetylation is especially well-known for controlling gene expression through histone modification, but it also regulates a wide range of non-histone proteins involved in cell signaling, metabolism, immune responses, and disease progression.
Protein acetylation is dynamically controlled by two main enzyme families: Lysine acetyltransferases (KATs), which catalyze the addition of acetyl groups, and Histone deacetylases (HDACs or KDACs), which remove acetyl groups. The balance between these enzymes determines acetylation levels and functional outcomes in the cell.
In addition to histones, many transcription factors, metabolic enzymes, chaperones, and cytoskeletal proteins are acetylated. Pathways often affected include gene regulation, mitochondrial metabolism, cell cycle control, and immune modulation. Acetylation can influence enzymatic activity, protein–protein interactions, and protein degradation.
Acetylation predominantly occurs on lysine (K) residues, and the modification is mass-incremented by +42.0106 Da. After trypsin digestion, acetylated peptides (Ac-peptides) are enriched using anti-acetyl-lysine antibodies and analyzed via high-resolution LC-MS/MS, allowing for site-specific identification and quantification.
Yes. All acetylated peptides are analyzed in an unbiased, proteome-wide manner, and annotation tools allow separate identification and functional categorization of histone vs. non-histone acetylation events, including site-level mapping and pathway enrichment.
Reference
Ree, R., Varland, S., & Arnesen, T. (2018). Spotlight on protein N-terminal acetylation. Experimental & molecular medicine, 50(7), 1–13. https://doi.org/10.1038/s12276-018-0116-z
