How to Detect Protein Acetylation

Protein acylation, namely protein acetylation, is one of the important and common post-translational modifications in eukaryotes. It refers to the process where the acetyl group of acetyl-CoA is covalently attached to the N-terminus or lysine residues of proteins under the action of acetyltransferase. Acetylation modification changes the structure of the original protein to a certain extent, further affecting its biological functions. It participates in the regulation of numerous life activities, such as DNA replication, gene expression, transcription, protein synthesis, stability, subcellular localization, and degradation. Studies have shown that acetylated proteins and their regulatory enzymes are closely related to aging and major diseases such as cancer and neurological disorders. Therefore, studying protein acetylation has special significance in revealing the molecular mechanisms of life activities and the pathogenesis of diseases.

The purpose of detecting protein acetylation is to determine whether acetylation occurs, at which amino acid sites it occurs, and the level of acetylation modification. The commonly used methods for detecting protein acetylation modifications are mainly based on immunoblotting (WB) and mass spectrometry (MS) analysis techniques. WB can achieve qualitative and quantitative identification of acetylated proteins. MS not only achieves qualitative and quantitative identification of acetylated proteins but also determines the acetylated amino acid sites, with sensitivity and accuracy higher than WB. WB is based on the specific binding of antigens and antibodies. Protein samples are first separated by polyacrylamide gel electrophoresis, then transferred to a solid-phase carrier and combined with an antibody (primary antibody), followed by an immunoreaction with a specially labeled secondary antibody. Detection is performed through methods such as autoradiography. Due to the low abundance of acetylated proteins under normal physiological conditions, mass spectrometry-based detection methods require the separation and enrichment of acetylated proteins before mass spectrometry analysis. The mass spectrometry data is then subjected to bioinformatics analysis to identify acetylated proteins.

BaiTaiPike Biotechnology uses the Thermo Fisher Q Exactive HF mass spectrometry platform combined with Nano-LC chromatography to provide rapid and efficientprotein acetylation modification analysisservice technology package. You only need to tell us your experimental goals and send us your samples. We will take care of all subsequent project matters, including protein extraction, protease digestion, acetylated peptide enrichment, peptide separation, mass spectrometry analysis, raw mass spectrometry data analysis, and bioinformatics analysis. Free consultation is welcome.

Submit Inquiry

Name *

Email Address *

Phone Number

Inquiry Project *

Project Description*

How to order?

Submit Inquiry