As all proteins on the Immunome protein array are correctly folded, they naturally conform into their correct native state upon immobilisation on the array. Hence they are functional, physiologically active and are able to carry out their specific roles and functions. For example:
- Kinases that are required to be present as homodimers are catalytically active, form homodimers, and autophosporylate in the presence of ATP.
- DNA binding proteins are able to bind fluorescently labelled DNA oligos.
Homodimers co-immobilised on the array
- On-chip phosphorylation assays demonstrate functionality of arrayed kinases.
- This example demonstrates that human kinases on the array are present as homodimers (as evidenced by autophosphorylation in the presence of ATP, which is required for catalytic activity).
Proteins naturally assemble
Many proteins exist in multimeric complexes, and will only function when individual monomers form a complete unit. Homodimers and tetramer components interact with each other on the array, and form functional complexes in which both conformational and linear epitopes are present.
- On-array trimers and tetramers form naturally on the Immunome protein array.
- Protein-protein interactions and disruptions can be quantified.