CCMS experiments provide a wide range of information such as the identification of protein interacting partners of captured proteins or post-translational modifications.

The isolated proteins can be analyzed and characterized further by gel electrophoresis or mass spectrometry.

This novel platform technology enables the identification and gel-free analysis of individual proteins and post-translational modifications based on mass spectrometry, and, in addition, the comparison of expression levles between population subsets.

All capture reactions are performed in a simple, homogeneous protocol that is amenable to automation and up-scaling with off-the-shelf liquid handling devices. CCMS experiments can be performed within a working day and the isolated proteins can be analyzed with standard methodology such as gel electrophoresis, tryptic digest and mass spectrometry. The CCMS process allows determining K_d values between the ligand and the affinity selected proteins which can be achieved by performing capture experiments with increasing Capture Compound™ to protein ratios, thereby shifting the equilibrium towards weaker ligand protein interactions. As a result of this experiment relative K_d values can be determined simply from the MS spectra. This step, literally, creates a snap shot of the enzyme / substrate equilibrium, thus generating initial information on the K_d.

 

The workflow for CCMS experiments is straightforward and can be easily automated.