Sorbitan monooleate (CAS 1338-43-8)

The Kinesin family of proteins comprises a diverse group of molecular motor proteins responsible for intracellular transport along microtubules, essential for various cellular processes. Members of this family share structural and functional similarities, characterized by a conserved motor domain containing ATPase activity and a coiled-coil tail region that interacts with cargo molecules. Kinesins are found in eukaryotic cells, and their primary role is to move organelles, protein complexes, and other cargo to specific destinations within the cell. One of the defining features of kinesin family members is their ability to function as microtubule motors. Microtubules are dynamic cytoskeletal filaments made of tubulin subunits, and kinesins interact with them to transport cargo. Kinesins are typically homodimeric proteins, where two identical motor domains are coupled through their tail regions. These motor domains hydrolyze ATP to generate mechanical force, allowing kinesins to walk along microtubules by converting chemical energy into mechanical work. Members of the kinesin family are involved in a wide range of intracellular processes, including the transport of organelles such as mitochondria, endoplasmic reticulum, and vesicles carrying cargo like neurotransmitters or proteins. Kinesins often function as part of multisubunit complexes, which include accessory proteins or adaptors that link kinesins to specific cargoes. KIF (Kinesin family) Inhibitors typically function by disrupting ATPase activity of Kinesins, and may exhibit broader activity against multiple Kinesin family members. Researchers utilize Kinesin inhibitors to dissect the roles of Kinesin motors in processes such as cell division, axonal transport, and organelle trafficking, shedding light on the intricate mechanisms that underlie these vital cellular functions.