Protein Post-Translational Modification (PTM) Omics Analysis

Over the past decades, researchers have discovered that the complexity of the human proteome far exceeds that of the genome. While approximately 20,000-25,000 human genes encode for over a million protein variants, this phenomenon arises from mechanisms such as gene recombination, selective transcription initiation, differential transcription termination, and splicing. Moreover, post-translational modifications (PTMs) play a crucial role in enhancing proteome complexity. PTMs significantly alter the physical and chemical properties of proteins by adding or removing specific chemical groups. These changes not only reshape the spatial configuration of proteins and regulate their activity states but also influence protein localization, folding stability within cells, and the construction of protein interaction networks.


As research progresses, post-translational modification has become a hot topic in the scientific community. Various PTMs such as phosphorylation, glycosylation, acetylation, and ubiquitination have garnered widespread attention due to their unique mechanisms of action. These modifications can have diverse effects on the functional properties of target proteins, sometimes leading to contrasting effects, thus playing crucial roles in cellular signaling, metabolic regulation, and disease development.

In addition to traditional antibody enrichment strategies, chemical/enzymatic labeling and metabolic labeling strategies have gradually been applied to the enrichment and identification of post-translational modifications. These emerging chemical proteomics analysis methods involve covalently linking specific molecular probes to target modifications or modified residues through chemical or enzyme-catalyzed reactions, enabling omics analysis. They demonstrate significant advantages in the study of low-abundance modifications such as palmitoylation, myristoylation, and glycosylation. Moreover, these strategies can be applied in live-cell systems, avoiding potential interferences caused by cell lysis-related oxidation.

Chomix possesses a comprehensive technical platform dedicated to fully supporting and efficiently assisting clients in conducting in-depth exploration and practice in the field of protein post-translational modification research. With our professional and advanced technical platforms, we are committed to providing clients with comprehensive and refined solutions to meet diverse needs and high precision requirements in protein post-translational modification research.



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1. Cysteine Post-Translational Modifications

Cysteine (Cys) is a common sulfur-containing amino acid in proteins, and its thiol group plays crucial roles in regulating molecular redox homeostasis, influencing enzymatic reactions, protein-protein interactions, and protein stability through diverse post-translational modification processes. Common post-translational modifications on cysteine include palmitoylation, nitrosylation, sulfenylation, and sulfonation. Colosseum Biosciences has developed universal probes or metabolic labeling strategies targeting cysteine residues and established corresponding chemical proteomics platforms for post-translational modification identification. This platform accurately identifies target proteins and modification sites of post-translational modifications.

2. Lysine Post-Translational Modifications

Lysine (Lys) is one of the amino acids with the most diverse post-translational modifications (PTMs) in the proteome. Reversible lysine post-translational modifications (Lys-PTMs) are common biochemical processes that play indispensable roles in regulating numerous critical cellular functions. Post-translational modifications on lysine include acetylation, succinylation, propionylation, butyrylation, crotonylation, malonylation, and lactylation. Colosseum Biosciences has developed a chemical proteomics technology platform based on chemical probes for lysine post-translational modifications, which accurately identifies target proteins and modification sites.

3. Serine/Threonine Post-Translational Modifications

Common post-translational modifications on serine (Ser) and threonine (Thr) mainly include phosphorylation, O-glycosylation, etc. These modifications significantly impact the activity state of proteins and their interactions with other molecules, playing important roles in various key biological processes. Therefore, the analysis of this type of post-translational modification is an important topic in protein function research. Colosseum Biosciences utilizes phosphorylation enrichment materials, non-natural glycan chemical probes, and other tools to accurately identify target proteins and modification sites for this type of post-translational modification.

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