Shaker (KV1) Channel Blocker Explorer Kit

K⁺ selective channels are some of the most widespread ion trafficking molecules in living organisms, with more than 70 genes encoding different K⁺ channels in humans. 38 of those genes encode members of the K_V channel super family¹. K_V channels are composed of two types of protein subunits: the α subunit, which forms the pore and auxiliary (β) subunits. α subunits tetramerize in order to form a functional K⁺ conducting channel. The K_V α subunit is a protein with six transmembrane (TM) domains and intracellular N- and C-termini. The most defined structural features are the extracellular loop between the fifth and sixth TM (which forms the K⁺ selectivity filter and the channel pore) and the fourth TM, which is positively charged and forms the voltage sensor of the protein².

The pharmacological profile of K_V channels is quite impressive. Due to the large number and types of functional K_V channels, it became very important to identify the different native K_V currents in different tissues, cell types and developmental stages. Therefore, molecules that can specifically bind K_V channel components have become powerful tools in characterizing both the channel structure and its physiological role. Peptidyl toxins, mainly from scorpion and snake venoms, play a major role in identifying the various K_V channels. Such toxins include dendrotoxins from the green and black mamba snakes and agitoxins from scorpions.