Anti-αII-Spectrin , cleavage-specific Antibody

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.

Our αII-Spectrin , cleavage-specific rabbit polyclonal primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat αII-Spectrin , cleavage-specific and is antigen affinity purified. It is great for use in WB.

A synthetic peptide (coupled to KLH) corresponding to amino acid residues around the calpain cleavage site, tyrosine 1176 in human αII-spectrin. This sequence has high homology with similar regions in rat and mouse αII-spectrin, but is not found in other spectrin family members.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

The antibody detects a 136 kDa* cleaved fragment corresponding to αII-Spectrin on SDS-PAGE immunoblots of mouse diaphram treated with thapsigargin. The antibody only detects cleaved αII-Spectrin and does not detect full length αII-Spectrin.