
Protein acetylation is one of the most significant forms of post-translational modifications. It refers to the process where an acetyl group is added to a lysine residue of a protein, catalyzed by acetyltransferases. Serving as a key mechanism for cells to control gene expression, protein activity, and physiological functions, this modification plays a vital regulatory role in protein structure and biological activity, representing a major pathway for the fine-tuning of protein function. Acetylation modifications are primarily categorized into two types: N-terminal acetylation and lysine acetylation. N-terminal acetylation mostly occurs in eukaryotic proteins and is catalyzed by N-acetyltransferases. Lysine acetylation, on the other hand, is a reversible process mainly catalyzed by lysine acetylases and deacetylases.
Recent studies indicate that acetylation modifications are not only crucial for influencing chromosomal structure and activating nuclear transcription regulators but are also widely involved in various key biological processes such as cell cycle regulation, metabolism, and actin polymerization. This modification is prevalent in human metabolic enzymes, regulating metabolic pathways and enzyme activity. Its role in metabolic control is highly conserved throughout evolution, present from prokaryotic cells to higher mammals.
We provide comprehensive and professional acetylation proteomics analysis services, including:
Our acetylation proteomics platform leverages a strategy that combines specific antibody enrichment with high-resolution mass spectrometry, ensuring efficient capture and accurate identification of acetylated peptides. Through optimized sample preparation protocols and a professional bioinformatics analysis pipeline, we achieve comprehensive detection and functional interpretation of acetylation sites across various sample types, delivering reliable data quality and profound biological insights to our clients.
Protein extraction and quantification are performed using standardized protocols tailored to the sample type.
Protein samples are digested using proteases such as Trypsin, with multi-enzyme strategies employed when necessary to increase coverage.
Acetylated peptides from the digest are enriched using specific antibodies via immunoaffinity purification.
Enriched peptides are separated by nano-liquid chromatography and analyzed by high-resolution mass spectrometry.
Raw MS data is acquired and processed using professional software for database searching and statistical analysis.
A comprehensive bioinformatics analysis is conducted on the identified acetylated proteins and sites to uncover their biological significance.
A detailed technical report is provided, including the experimental procedure, MS parameters, identification results, and bioinformatics analysis.
To ensure accurate experimental results, please refer to the following sample requirements:
| Sample Type | Minimum Amount Required |
| Plant Leaves | Wet weight ≥ 0.8 g |
| Plant Roots, Stems, Xylem, Phloem, etc. | Wet weight ≥ 10 g |
| Cell Samples | Cell count equivalent to wet weight ≥ 8×10⁷ |
| Tissue Samples (Human, Animal, Microbial) | Wet weight ≥ 300 mg |
| Body Fluid Samples | Serum/Plasma volume ≥ 1 ml, CSF ≥ 1 ml, Urine ≥ 50 ml |
All samples should be stored in liquid nitrogen or at -80°C and shipped with an adequate amount of dry ice to avoid repeated freeze-thaw cycles.
Acetylation proteomics provides a powerful tool for deciphering the fine-tuned regulation of life processes. We look forward to offering you professional and reliable technical support for your research, exploring the mysteries of protein modifications together.