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Anti-αII-Spectrin , cleavage-specific Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q13813 |
|---|---|
| Reactivity | Bovine |
| Host | Rabbit |
| Clonality | Rabbit Polyclonal |
| Isotype | IgG |
| Calculated MW | 284539 Da |
| Gene ID | 6709 |
|---|---|
| Other Names | Alpha-II spectrin, Fodrin alpha chain, Spectrin, non-erythroid alpha subunit, SPTAN1, NEAS, SPTA2 |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Anti-αII-Spectrin , cleavage-specific Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
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Provided below are standard protocols that you may find useful for product applications.
Background
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-spectrin I and β-spectrin I form heterodimers in red blood cells, while nonerythroid mammalian cells contain heterodimers of α-spectrin I and II with β-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. α-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. 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.
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