Eta;-Spectrin Ii Mouse, Unlabeled, Clone: 42, Bd, Mouse Monoclonal Antibody, Each

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Spectrins are central components of the cytoskeleton that form a scaffold below the plasma membrane. Spectrins contain two subunits, α and β, which intertwine to form heterodimers that can self associate into elongated tetramers. Α-spectin i and β-spectrin i form heterodimers in red blood cells, while nonerythroid mammalian cells contain heterodimers of α-spectin i and ii with β-spectrin i to v. The structure of spectrins includes a succession of triple-helical repeats alongwith various domains, such as sh3 domain, ef hands, ph domains, and binding domains for ankyrin, actin, band 4.1, And calmodulin. Α-spectrin ii is a widely expressed non-erythroid α-spectrin that contains an sh3 domain, a calmodulin binding site, and two cleavage sites for proteases, such as calpains and caspase-3. Β-spectrin ii is a widely expressed non-erythroid β-spectrin that contains a c-terminal region that interacts with α-spectrins and a ph domain. Α-spectrin ii and β-spectrin ii, like many other spectrins, can form heterodimers that can self associate into tetramers, as well as interact with band 4.1, F-actin, and other proteins near the plasma membrane. This scaffold of cytoskeletal and plasma membrane proteins is critical for the maintenance of cell structure.Immunofluorescence, western blotting