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α-Spectrin II Mouse, Unlabeled, Clone: 35, BD
Mouse Monoclonal Antibody
Specifications
Antigen | α-Spectrin II |
---|---|
Clone | 35 |
Concentration | 250μg/mL |
Applications | Immunofluorescence, Western Blot |
Classification | Monoclonal |
Description
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 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 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
Specifications
α-Spectrin II | |
250μg/mL | |
Monoclonal | |
Mouse | |
Cell Biology | |
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide. | |
IgG1 | |
Affinity Purified |
35 | |
Immunofluorescence, Western Blot | |
Unconjugated | |
RUO | |
Canine, Chicken, Human | |
Human α-Spectrin II aa. 252-371 | |
Primary |
For Research Use Only.
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