Anti-alphaII-Spectrin , cleavage-specific Antibody, Rabbit, Polyclonal
Artikelnummer:
ABT-AN1966
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| Artikelname: | Anti-alphaII-Spectrin , cleavage-specific Antibody, Rabbit, Polyclonal |
| Artikelnummer: | ABT-AN1966 |
| Hersteller Artikelnummer: | AN1966 |
| Alternativnummer: | ABT-AN1966-100UL |
| Hersteller: | Abcepta |
| Wirt: | Rabbit |
| Kategorie: | Antikörper |
| Alternative Synonym: | Alpha-II spectrin, Fodrin alpha chain, Spectrin, non-erythroid alpha subunit, SPTAN1, NEAS, SPTA2 |
| Spectrins are central components of the cytoskeleton that form a scaffold below the plasma membrane. Spectrins contain two subunits, alpha and beta, which intertwine to form heterodimers that can self associate into elongated tetramers. alpha-spectrin I and beta-spectrin I form heterodimers in red blood cells, while nonerythroid mammalian cells contain heterodimers of alpha-spectrin I and II with beta-spectrin I to V. The structure of spectrins includes a succession of triple-helical repeats along with various domains, such as SH3 domain, EF hands, PH domains, and binding domains for ankyrin, actin, band 4.1, and calmodulin. alpha-spectrin II is a widely expressed non-erythroid spectrin that contains an SH3 domain, a calmodulin binding site, and two cleavage sites, one at Tyr-1176 for calpains and one at Asp-1185 for caspase-3. alpha-spectrin II and beta-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. |
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