Bta-Spectrin II Pure 42 150ug

Spectrins are central components of the cytoskeleton that form a scaffold below the plasma membrane. Spectrins contain two subunits, α and

ß, which intertwine to form heterodimers that can self associate into elongated tetramers. α-spectin I and ß-spectrin I form heterodimers in red

blood cells, while nonerythroid mammalian cells contain heterodimers of α-spectin I and II with ß-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. ß-spectrin II is a widely expressed non-erythroid

ß-spectrin that contains a C-terminal region that interacts with α-spectrins and a PH domain. α-spectrin II and ß-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.

1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.

2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.