The underlying motivation of the work is to reveal the non-equilibrium adhesion mechanics of a disordered elastomeric protein (Squid ring teeth, SRT), its phase kinetics as solid aggregates (similar to amyloids), and physical properties as colloidal suspensions (i.e., globular proteins). Most proteins adhere strongly to wet interfaces as monolayers (i.e., adhesive), but they are not known to be effective in chemically bonding together two substrates (i.e., cohesive as well as adhesive). Special proteins from marine organisms, such as blue mussels, acorn barnacles, sandcastle worms and freshwater caddisfly larva provide underwater adhesion due to modified amino acid chemistry or coacervation. Micro-scale roughness, crack trapping, wetting transitions also help the adhesion of land animals (e.g., adhesion of lizard or insects footpads). However, SRT does not function as adhesive in nature (i.e., it is a structural protein which strengthen the squid tentacles for holding the prey), and the adhesion mechanism of SRT could not be explained by equilibrium mechanics. Key aspects of the temperature effect on SRT, its adhesion mechanics based on nanoscale domain instability combined to surface chemistry will be discussed.