Anti-Ankyrin-B Antibody, clone N105/13 clone N105/13, from mouse

Ankyrin-2 (UniProt Q01484; also known as ANK-2, Ankyrin-B, Brain ankyrin, Brank-2, Non-erythroid ankyrin) is encoded by the ANK2 (also known as LQT4) gene (Gene ID 287) in human. Ankyrins are scaffold proteins that play essential roles in providing plasma membrane with mechanical support and in controlling excitable tissues by connecting numerous ion channels, cell adhesion molecules, and receptors to the spectrin-based cytoskeleton. There are three human ankyrins (ankyrin-R, -B, and -G encoded by ANK1, ANK2, and ANK3 gene, respectively), all share similar domain organization, including an N-terminal membrane-binding domain composed of 24 ankyrin (ANK) repeats, a spectrin-binding region comprised of two ZU5 domains, a UPA domain, a death domain (DD) and a variable C-terminal regulatory domain. The three ankyrins, however, do have distinct and non-overlapping functions in specific membrane domains coordinated by ankyrin-spectrin networks. Ankyrins mediate a wide range of physiological functions by interacting with and anchoring numerous membrane targets to specific membrane micro-domains in coordination with spectrin-based cytoskeletal structures. Examples include AnkB-mediated coordination of voltage-gated sodium channels, Na+/K+- ATPase, Na+/Ca2+ exchanger, and inositol 1,4,5-triphosphate receptors in cardiomyocytes, as well as the dystrophin/dystroglycan complex in skeletal muscles. In addition, multiple ankyrin isoforms generated through alternative splicing of a given ANK gene can further impart functional specificity and distinct subcellular distribution.