Protein Methylation Service


Protein methylation is a post-translational modification (PTM) process, in which highly specific enzymes called methyltransferases are responsible for the addition of methyl groups to a targeted molecule and S-adenosyl methionine (SAM) as the primary donor of methyl group. Protein methylation commonly occurs on arginine, lysine, histidine, proline, and carboxyl groups. Protein methylation plays an important role in modulating cellular and biological processes, including transcriptional regulation, RNA processing, metabolism and signal transduction.

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Figure 1. Types of methylation on arginine residues (Yang Y and Bedford M T, 2013).

Overview of Protein Methylation Service

Creative Proteomics has already developed a highly sensitive HPLC-MS/MS pipeline that can analyze N- and O-methylation. With powerful and sensitive tools, we can identify, quantify and characterize protein methylation. Metabolic labeling strategies can be coupled with MS to measure dynamic and differential in vivo protein methylation rates. In addition, we also provide bioinformatics services in Protein Post-translational Modification Analysis. We have optimized our protocol to enable more fast and sensitive services for methylation analysis. Shown as Figure 2, our protein methylation service contains digestion, enrichment, LC-MS/MS analysis, and data analysis. 

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Figure 2. The workflow of protein methylation analysis. 

Sample Requirements

If you want to know specific samples requirements, please feel free to contact us.

Delivery

Our Advantages

Technology platforms

Matrix Assisted Laser Desorption Ionization Mass Spectrometry (MALDI-MS)

At Creative Proteomics, many excellent and experienced experts will optimize the experimental protocol according to your requirement and guarantee the high-quality results for protein methylation analysis. As every project has different requirements, please contact our specialists to discuss your specific needs. 


Reference

1. Yang Y, Bedford M T. Protein arginine methyltransferases and cancer. Nature Reviews Cancer, 2013, 13(1): 37.



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