In the study of acetylation modification of proteins, in addition to determining the presence of acetylation of target proteins and performing the identification and quantification of acetylation, it is essential and important to resolve the effects of acetylation on target proteins as well as to explore the biological functions of acetylation of target proteins. Creative Proteomics also specializes in providing bioinformatic acetylomics data analysis services. Our professional experts have established robust and effective bioinformatics workflows for the analysis of lysine acetylation. We are committed to providing a variety of bioinformatics analysis and custom services to meet the diverse needs of our clients.
Protein acetylation is the process of adding acetyl groups to the lysine residues of proteins by the action of acetyltransferases, a mechanism by which cells control gene expression, protein activity, or physiological processes. The function of acetylation is mainly focused on the effect on cellular chromosome structure and the activation of transcriptional regulators in the nucleus. In recent years, it has been found that a large number of non-nuclear proteins are modified by acetylation under physiological conditions, with a wide range of biological significance.
We have years of experience in large-scale proteomics research and post-translational modification (PTM) proteomics analysis. We have established an industry-leading platform for PTM proteomics analysis based on advanced bioinformatics analysis methods. The MS data is processed using an effective and systematic lysine acetylomics bioinformatics workflow developed at our platform. Our bioinformatics analysis contents include:
Creative Proteomics serves as a global leader in PTM proteomics analysis. We are driven by customer needs, a solid scientific basis, and innovative technologies to advance and develop scientific research. If you are interested in our protein acetylation identification service, please feel free to contact us for information.
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