Protein arginine methylation is an essential post-translational modification that regulates protein function and is a post-translational modification (PTM) catalyzed by a family of nine enzymes called protein arginine methyltransferases (PRMT). Methylation of histone arginine sites plays a vital role in the regulation of gene transcription. It affects a variety of physiological processes in cells, including DNA repair, signaling, and cell development. Lifeasible's large-scale analysis of protein arginine methylation using methylation modification proteomics and mass spectrometry provides an ideal analytical strategy to study the extent of arginine-methylation of proteins in model systems and identify PRMT targets.

Large-scale methylation modification proteomics

Arginine methylation (Me-R) antibodies are available for methylated peptide enrichment for methylated proteomic analysis. Depending on the number of methylation modifying groups contained on the amino acid residues, Me-R antibodies include MMA antibodies, ADMA antibodies, and SDMA antibodies. The various types of antibodies for Me-R need to be used separately.

After enrichment of methylated peptides using specific antibodies against different methylation sites and modification forms, we can achieve quantitative and qualitative analysis of large-scale methylated proteins in combination with LC-MS/MS analysis. Just tell us your experimental purpose and send us the samples; we will provide a one-stop service including protein extraction, proteolytic cleavage, methylated peptide enrichment, peptide isolation, mass spectrometry analysis, mass spectrometry raw data analysis, and bioinformatics analysis.

Bioinformatics analysis

• Mass spectrometry data quality analysis
• Statistical analysis of significant differences
• Gene Ontology annotation and enrichment analysis
• KEGG annotation and enrichment analysis
• Protein interactions network PPI analysis
• Protein modification PTM analysis

Sample requirements

• Plant leaves and other fresh tissues ≥ 5 g wet weight.
• Plant impurity-rich or low protein content samples such as plant roots, rhizomes, xylem, and phloem tissues ≥ 10 g dry weight.
• Plant pollen ≥ 400 mg.

Technology platforms

• Ion chromatography
• High-performance liquid chromatography (HPLC)
• Matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS)

Technical advantages

• High throughput. Up to thousands of proteins can be identified and quantified at one time.
• 100% coverage. Proteolytic cleavage using 2-3 enzymes to ensure complete coverage.
• Can be used to analyze low-abundance methylation-modified proteins.
• High resolution and sensitivity mass spectrometer.

Arginine methylation regulates histone function and is involved in the epigenetic regulation of gene transcription. Lifeasible conducts a proteomic analysis of methylation modification in different groups of samples provided by clients, identifies methylation modification sites/peptides/proteins in all samples, quantitatively screens for significant differential expression of methylation modification sites between different groups of samples, and performs bioinformatics analysis of related methylation modification proteins. Please feel free to contact us for more information.

*If your organization requires the signing of a confidentiality agreement, please contact us by email.

For research use only, not intended for any clinical use.

Related Services

• Histone Variants and Histone Modifications
• Histone Associated Chaperone Proteins