The chemical modifications of proteins that occur after biosynthesis are referred to as post-translational modifications (PTM), which typically result in changes to the characteristics and functions of the proteins. PTMs include the attachment of functional groups, such as methylation, acetylation, glycosylation and phosphorylation, covalent coupling of small peptides or proteins, such as ubiquitination and SUMO,  or chemical changes to amino acids, such as citrullination (conversion of arginine to citrulline). Protein modifications play a crucial role in cellular physiological processes, and the function of proteins can vary under different modification states. Moreover, the same modification at different sites may have completely different effects on protein function.

The challenge in detecting and identifying protein site modifications necessitates the use of highly specific antibodies for discrimination. Currently, most antibodies available on the market for small molecules and modifications are rabbit-derived polyclonal or monoclonal antibodies (data source: CiteAb official website using modification type keywords).

Rabbit-derived antibodies, known for their high sensitivity and smaller epitope recognition, are more suitable for developing antibodies targeting protein modification sites compared to mouse-derived antibodies, especially for small molecule modification antibodies. Leveraging our proprietary rabbit single B cell antibody development platform, we offer one-stop development services for protein modification antibodies.