Cephalopods have recently emerged as a source of inspiration for the development of novel functional materials. Within this context, a number of studies have explored structural proteins known as reflectins, which play a key role in cephalopod adaptive coloration in vivo and exhibit interesting properties in vitro. Herein, we report an improved high-yield strategy for the preparation and isolation of reflectins in quantities sufficient for materials applications. We first select the Doryteuthis (Loligo) pealeii reflectin A2 (RfA2) isoform as a "model" system and validate our approach for the expression and purification of this protein. We in turn fabricate RfA2-based twoterminal devices and employ both direct and alternating current measurements to demonstrate that RfA2 films conduct protons. Our findings underscore the potential of reflectins as functional materials and may allow a wider range of researchers to investigate their properties.Cephalopods (squid, octopuses, and cuttlesh) are well known for their sophisticated neurophysiology, complex behavior, and stunning camouage displays.1-6 Recently, these animals have drawn signicant attention as sources of novel materials for optical systems, 7-10 biomedical technologies, 11-15 and bioelectronic devices. [16][17][18][19][20] Within this context, a number of literature reports have investigated the properties of unique structural proteins known as reectins, [7][8][9][10]14,[16][17][18][21][22][23][24] which are found in cephalopod skin cells (i.e. leucophores, iridophores, and chromatophores). [25][26][27][28][29][30] In vivo, reectins in general have been shown to play important roles in cephalopod adaptive coloration by serving as components of optically-active ultrastructures, including layered stacks of membrane-enclosed platelets in iridophores, 25,26 membrane-bound arrangements of spherical microparticles in leucophores, 27,28 and interconnected networks of pigment granules in chromatophores. 29,30 In vitro, the Doryteuthis (Loligo) pealeii reectin A1 (RfA1) isoform has found applications in recongurable infrared camouage coatings that are actuated by chemical and mechanical stimuli, 7,8 proton-conducting lms with electrical gures of merit rivaling those of some articial analogues, 16-18 and biocompatible substrates that support the proliferation and differentiation of neural stem cells.14 Overall, reectins' fascinating properties have provided a strong impetus for their continued exploration from both fundamental and applied perspectives.Herein, we describe an improved methodology for the production of difficult-to-handle reectins in quantities sufficient for materials applications. We rst select the Doryteuthis (Loligo) pealeii reectin A2 (RfA2) isoform as a "model" system for electrical characterization and validate a new high-yield strategy for the expression and purication of this precipitation-prone protein. We subsequently fabricate and characterize two-terminal devices for which RfA2 thin lms constitute the active layer. We in tu...