The occurrence of toxic proteins in various sources like microorganisms, snake venoms, fish venoms etc have created an intense curiosity and formulation of research to study them. Boxin is one such toxic protein that is less widely known and appreciated. Boxin is a stable, heat and trypsin resistant toxic protein isolated from the crude defensive skin secretions of boxfishes by cold acetonic precipitation and RP-HPLC chromatography. The molecular weight of boxin is reported to be 18 kDa which is known from laser desorption induced time of flight mass spectrophotometry. Boxin has an UV absorbance at 254 nm and 280 nm. In ichthyotoxic front, boxin is 33 times more potent than pahutoxin, which is associated with boxin in the skin secretions. Boxin is known to be the representative of protein fractions found in the toxic mucus of boxfishes. It contributes about 3% of the total ichthyotoxicity to the skin secretion. Apart from boxin, the other protein fractions in the secretions are chemically distinct entities which are reported to be the enhancers of ichthyotoxicity and chelators of pahutoxin performing allomonal roles in the marine environments, due to their high chemical stability and protein nature which ensures them resistance in harmful environments and solubility in sea water. In short, these proteins are ideal candidates which can replace other allomones for cooperative interactions with functional significance.