Protein acetylation is one of the major post-translational modifications (PTMs) in eukaryotes, and studies have shown that acetylated proteins are involved in a variety of cellular processes, such as translation, transcription, protein folding, cell division, DNA damage repair, signal transduction, and metabolism. Creative BioMart's extensive experience in post-translational modification of proteins based on computational and experimental methods enables us to provide protein acetylation service to accelerate your project.

Protein acetylation refers to the introduction of the acetyl group of acetyl coenzyme A (Ac-CoA) into a specific site on the polypeptide chain. Most eukaryotic proteins and regulatory peptides are acetylated at amino-terminal residues, whereas lysine acetylation occurs at different sites in different proteins, including histones and transcription factors. Acetylation of proteins can affect their charge, conformation, stability, localization, synthesis, and interactions with other molecules. Studies have shown that single lysine changes on histones significantly affect cellular homeostasis, as the acetylation state of histones regulates various transcription factors, molecular chaperones, and cellular metabolism. Furthermore, the regulation of histone acetylation by histone acetylases (HATs) or histone deacetylases has been clearly linked to aging and various neurological and cardiovascular diseases. Therefore, protein acetylation is also a promising target for the development and design of new drugs for many diseases in recent years.

Fig 1. Nt-acetylation has many functions in the cell. (Ree R, et al., 2018)

Services

There are currently three well-known forms of acetylation: Nα-acetylation, Nε-acetylation and O-acetylation. In recent years, due to the wide application of mass spectrometry and the emergence of new technologies such as protein chips, the research on protein acetylation has been further developed. Creative BioMart has successfully and reliably studied protein acetylation using a variety of techniques, with a good understanding of protein acetylation status, allowing characterization of the temporal regulation and stoichiometry of individual acetylation sites. In addition, our scientists are committed to developing some computational models to predict acetylation sites.

Advanced mass spectrometry techniques combined with informatics enable the localization of numerous acetylation sites in all proteins. We uncover the biological consequences and mechanisms of acetylation by combining in vivo characterization, in vitro biochemical and proteomic analyses. We provide the following services for protein acetylation, including but not limited to:

• Identification and qualitative assessment of acetylation: with the help of high-resolution mass spectrometry-based proteomics, it is possible to not only identify specific acetylation sites, but also quantitatively characterize the acetylome and determine relative proteins in various treatments and genetic mutants How acetylation abundance changes dynamically.
• Stoichiometry or occupancy of acetylation sites: we used stoichiometric assessments to identify acetylation sites that may have a significant effect on protein function.
• Analyzing acetylation modification interactions and crosstalk: using mass spectrometry to study acetylation modification crosstalk by comprehensively characterizing multiple PTMs in a single protein sample.

Approaches for Analyzing Protein Acetylation

• Identification of acetylation modification sites by biological mass spectrometry.
• Recognition of acetylated lysine residues based on specificity.
• Acetylated antibody identification.
• Identification of acetylation modification sites by a labeled substrate-based approach.
• Mass spectrometry-based proteomics approach.
• Bioinformatics.

Our mission is to provide global customers with the most comprehensive and professional customized protein acetylation service. If you have any special requirements about our services, please feel free to contact us. We are looking forward to working together with your attractive projects.

References

1. Ree R, Varland S, Arnesen T. (2018) Spotlight on protein N-terminal acetylation. Exp Mol Med. 50(7):1-13. 
2. Drazic A, Myklebust LM, Ree R, Arnesen T. (2016) The world of protein acetylation. Biochim Biophys Acta. 1864(10): 1372-1401.

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