Propionylation Analysis Service

Gene expression in eukaryotes is tightly regulated, on the one hand by transcription factors; on the other hand, it is regulated at the epigenetic level. Histone modifications are an important part of epigenetics, and with the rapid development of high-resolution mass spectrometry, novel histone modifications can be identified. Among them, lysine propionylation modification is an important reversible post-translational modification of histone proteins discovered in recent years, which is widely involved in a series of biological processes and cellular metabolic pathways in prokaryotes and eukaryotes. In addition, propionylation modification has also been found to play an important role in the overall metabolic regulation network of bacteria and the activity regulation of metabolic enzymes, the cellular stress response of bacteria and mammals, the epigenetic regulation of eukaryotes and prokaryotes, as well as the regulation of photosynthesis.

Propionylation is the process of covalent binding propionyl groups (e.g., propionyl coenzyme A and other donors) to lysine residues in substrate proteins catalyzed by the action of acyltransferases (e.g., acetyltransferases).

Our Propionylation Proteomics Service

Creative proteomics offers the lysine propionylation modification service to identify propionylated proteins and their modification sites using high-resolution tandem mass spectrometry complementing the enrichment strategy.



Customized Bioinformatics Services

Sample requirements



Technology platform

Ion Chromatography
High-Performance Liquid Chromatography (HPLC)
Matrix-Assisted Laser Desorption Ionization Mass Spectrometry (MALDI-MS)

1. Adam F Kebede, et al. Histone propionylation is a mark of active chromatin. Nature structural & molecular biology.(2017).

* For Research Use Only. Not for use in diagnostic procedures.
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