Honey bee as apitoxin, carries several active components, the most abundant of which is melittin, and the most biologically active are enzymes, particularly phospholipase A2. Bee venom is under laboratory and clinical research for its potential properties and uses in reducing risks for adverse events from bee venom therapy, rheumatoid arthritis, and use as an immunotherapy for protection against allergies from insect stings. Bee venom products are marketed in many countries, but, as of 2018, there are no approved clinical uses for these products which carry various warnings for potential allergic reactions. With an increased number of honey bees in a specific
Evolution of snake venom highly venomous caenophidian snakes (also referred to as "colubroidian snakes"), thus suggesting that most venom evolution took place after this lineage diverged from other snakes. The primary mechanism for the diversification of venom is thought to be the duplication of gene coding for other tissues, followed by their expression in the venom glands. The proteins then evolved into various venom proteins through natural selection. This process, known as the birth-and-death model, is responsible for several of the protein recruitment events in snake venom. These duplications occurred in a variety of tissue types with a number of ancestral functions. Notable examples