Acetylproteomics Analysis Service
- Our platform is compatible with various sample types: cells, tissues, plasma/serum, and other biofluids.
- Standardized lysis and protein extraction with rigorous quality control (BCA quantification/SDS-PAGE validation).
- Immunoaffinity enrichment (anti-acetyllysine antibodies) or chemical acyl-exchange techniques are ued to enhance the capture efficiency of low-abundance acetylated peptides.
- High-abundance interfering proteins (e.g., albumin and immunoglobulins in blood samples) are removed to reduce background noise.
- High-end mass spectrometers such as Orbitrap Exploris™ 480, coupled with data-dependent acquisition (DDA) or data-independent acquisition (DIA) for deep and broad coverage of acetylation sites.
- Optimized mass spectrometry parameters (MS1/MS2 resolution >120,000) ensure precise identification of modified peptides in complex samples.
- Qualitative (site identification) and quantitative (labeled/label-free) analysis are provided based on research needs.
- Custom bioinformatics analysis: differential acetylation protein screening, functional enrichment (GO/KEGG), protein interaction network construction, and more.
- Revealing acetylation-regulated pathways involved in cancer metastasis (e.g., Wnt/β-catenin, NF-κB).
- Analyzing histone acetylation-driven epigenetic reprogramming mechanisms.
- Identifying novel prognostic biomarkers (e.g., specific acetylated proteins in circulating tumor cells) and predictive markers for histone deacetylase inhibitors (HDACi) therapy response.
Acetylation is a crucial post-translational modification (PTM) that dynamically regulates protein stability, subcellular localization, enzymatic activity, and interaction networks by adding acetyl groups to lysine (K) residues, N-terminal amino acids, or specific serine/threonine (O-acetylation) sites. This modification is widely involved in cellular metabolic reprogramming, chromatin remodeling, signal transduction, and immune regulation, and is closely associated with the development of cancer, neurodegenerative diseases, and metabolic syndromes.
Diallo, I. et al. Expert Rev Proteomics. 2019.
Figure 1. Different Types of Protein Acetylation: (a) Nter Acetylation, (b) K-Acetylation and (c) O-Acetylation
Acetylproteomics is an advanced approach for systematically characterizing acetylation sites, their dynamic changes, and biological functions. It relies on high-sensitivity mass spectrometry (MS) combined with targeted enrichment strategies to achieve qualitative and quantitative analysis of protein acetylation at the proteome-wide level. However, the low abundance and dynamic nature of acetylation, sample complexity (e.g., blood and tissues), and challenges in site identification accuracy necessitate highly specialized and stable analytical workflows.
Pascovici, D. et al. Int J Mol Sci. 2018.
Figure 2. The Workflow of Protein PTM Analysis
MtoZ Biolabs provides professional acetylproteomics analysis service for scientific and clinical research. Leveraging state-of-the-art mass spectrometry platforms and optimized workflows, we help researchers accurately capture acetylation sites in samples, uncover their regulatory roles in physiological processes and disease progression, and facilitate target discovery and translational medicine research.
Analysis Workflow
Our one-stop acetylation analysis workflow integrates sample processing, targeted enrichment, and deep proteomic analysis to ensure data reliability and high-dimensional output:
1. Sample Preparation and Quality Control
2. Efficient Enrichment of Acetylated Peptides
3. High-Resolution Mass Spectrometry Analysis
4. Data Analysis and Functional Annotation
Why Choose MtoZ Biolabs?
1. Ultra-Sensitive Detection
Optimized enrichment strategies combined with proprietary mass spectrometry methods enable detection of acetylated peptides at femtomole levels, covering over 99% of known modification types.
2. Expertise in Complex Sample Processing
Standardized workflows for contaminant removal and enrichment significantly enhance site detection rates in high-interference samples such as blood and tumor tissues.
3. Fully Standardized Workflow
Our service adheres to ISO-certified quality management systems, ensuring full traceability from sample reception to data delivery and guaranteeing reproducibility.
4. Customizable Service Solutions
Flexible experimental designs tailored to specific research objectives, with integrated multi-dimensional data analysis support.
5. Rapid Turnaround Time
Routine projects are completed within 3-5 weeks, with expedited services available for urgent cases.
Applications
Acetylproteomics offers new perspectives for disease mechanism research and precision medicine. Our acetylproteomics analysis service can be applied in various fields:
1. Cancer Research
2. Hematological Diseases
Investigating aberrant acetylation modifications driving apoptosis resistance or metabolic evasion in leukemia cells, supporting combination therapy strategies.
3. Neurodegenerative Diseases
Exploring tau protein acetylation in neurofibrillary tangle formation, advancing research in Alzheimer's disease pathology.
Case Study
1. Quantitative Acetylomics Reveals Dynamics of Protein Lysine Acetylation in Mouse Livers During Aging and Upon the Treatment of Nicotinamide Mononucleotide
Lysine acetylation is a reversible post-translational modification that plays a crucial role in regulating cellular processes such as aging. However, acetylome-wide analysis in mammalian tissues remains limited. This study employs two antibodies for the enrichment of acetylated peptides and performs label-free quantitative acetylomic analysis to investigate the dynamics of protein acetylation in mouse livers during natural aging and after treatment with β-nicotinamide mononucleotide (NMN). The findings reveal previously unknown acetylation sites and identify potential aging biomarkers. Additionally, the study suggests that NMN's beneficial effects on health span are linked to age-related changes in protein acetylation, though its impact on known Sirtuin substrates is relatively mild. This research lays a foundation for further functional studies of protein post-translational modifications in aging and disease. Acetylproteomics Analysis Service provides high-sensitivity mass spectrometry-based acetylproteomics analysis, utilizing optimized enrichment strategies to enhance the detection of low-abundance acetylation modifications. It enables the study of dynamic changes in protein acetylation during aging and the evaluation of regulatory factors affecting acetylation, offering valuable data support for in-depth exploration of post-translational modifications.
Li, J. et al. Mol Cell Proteomics. 2022.
Figure 3. Acetylome Studies Reveal Previously Uncharacterized Protein Acetylation in Mouse Livers
2. Global Profiling of Ribosomal Protein Acetylation Reveals Essentiality of Acetylation Homeostasis in Maintaining Ribosome Assembly and Function
Acetylation is a widespread post-translational modification involved in cellular regulation. This study systematically profiled ribosomal protein acetylation in Salmonella Typhimurium, identifying 289 acetylated lysine residues in 52 ribosomal proteins. The findings indicate that acetylation, mediated by the acetyltransferase Pat and acetyl phosphate, is essential for ribosome assembly by modulating ribosomal protein binding to rRNA. Additionally, proper acetylation levels are critical for interactions between elongation factors and polysomes, as well as for maintaining translation efficiency and fidelity. Dysregulation of acetylation alters bacterial sensitivity to ribosome-targeting antibiotics, highlighting the role of acetylation homeostasis in ribosome function and its potential as a universal regulatory mechanism. Acetylproteomics Analysis Service enables comprehensive profiling of protein acetylation. By applying optimized enrichment strategies, it facilitates the identification of acetylation sites and their regulatory mechanisms. The service supports research on protein acetylation dynamics, providing valuable insights into post-translational modifications.
Ni, J. et al. Nucleic Acids Res. 2023.
Figure 4. Lysine Acetylation in r-Proteins is Detected
Deliverables
1. Raw Data and Identification Results: Comprehensive information on identified acetylation sites, stoichiometry, and mass spectrometry validation spectra.
2. Quantitative Analysis Reports: Differentially acetylated protein lists (Fold Change/p-value), clustering heatmaps, and functional annotation networks.
3. Expert Interpretation Support: In-depth data analysis and experimental optimization guidance to accelerate research translation.
Protein acetylation dynamics represent a "blueprint" for understanding cellular regulation in health and disease. High-precision acetylproteomics is the key to decoding this intricate modification network. With cutting-edge expertise and a deep understanding of clinical research needs, MtoZ Biolabs is committed to delivering reliable and efficient acetylproteomics solutions for researchers worldwide. Whether you are exploring fundamental mechanisms or developing innovative therapeutics, we provide rigorous methodologies and advanced technologies to help unlock the biological significance of acetylation. Contact MtoZ Biolabs today to embark on your next acetylation research breakthrough!
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