Solids can be stable above their melting equilibrium temperature in a meta-stable superheated state. In contrast to the supercooling of liquids, the superheating of solids is not easily achieved due to the tendency of the surface to melt, even below the melting temperature. Antifreeze proteins are a class of ice binding proteins (IBPs) that are found in many cold-adapted organisms, where they serve as inhibitors of ice crystal growth. IBPs stop ice crystal growth by binding to the ice surface. It was argued that surface-adsorbed IBPs should also prevent ice from melting and thus impose a superheating state, but to date this has been demonstrated only in a qualitative manner. We measured the superheating of ice crystals that were stabilized by IBPs. The ability of the IBPs to prevent ice melting suggests that the proteins adhere irreversibly to the ice surface. Further support for this suggestion comes from our investigation of ice growth in the presence of IBPs using fluorescence microscopy and microfluidic devices. The control over ice growth has a tremendous potential in preventing frost damage to plants, in cryo-preservation of cells, tissues and organs, and in the food industry.