Rabbit Polyclonal Antibody to αII-Spectrin Cat# RPCA-aII-Spec

      Spectrin family molecules are important high molecular weight components of the submembranous cytoskeleton of eukaryotic cells. These proteins were isolated originally from lysed red blood cell membrane preparations which were named "ghosts", which gave rise to the name spectrin (1). Spectrin family molecules are mostly composed of spectrin repeats, compact ~110 amino acid modules made of three closely packed α-helices, though they may also include SH3 domains, PH domains, EF hands and other important binding sites. They function as major components of the membraneous cytoskeleton, mediating interactions between integral membrane proteins, actin and many other cellular components. The RPCA-aII-Spec antibody binds specifically to αII-spectrin, also known as non-erythroid spectrin or fodrin (2-4). In the CNS this protein is expressed only in neurons and so the antibody can be used to reveal the submembranous neuronal cytoskeleton in IF, ICC and IHC. Defects in spectrin genes present as a variety of diseases (5,6). The molecule is subject to proteolysis by calpain producing a 150kDa and 145kDa C-terminal fragments and by caspase producing a slightly different 150kDa C-terminal fragment and a 120kDa C-terminal fragment. Since caspase activation is characteristic of apoptosis and calpain activation of necrosis, it may be possible to use selective monitoring of each type of cell death by monitoring the content of these protein fragments (7).

      This antibody has been tested on formalin fixed and paraffin embedded samples for IHC, and is not recommended for this purpose.

1. Marchesi VT, Steers E. Selective solubilization of a protein component of the red cell membrane. Science 159:203-4 (1968).
2. Levine J, Willard M. Fodrin: axonally transported polypeptides associated with the internal periphery of many cells. J. Cell Biol. 90:631-42 (1981).
3. Bennett V, Baines AJ. Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. Physiol. Rev. 81:1353-92 (2001).
4. Djinovic-Carugo K, Gautel M, Ylänne J, Young P. The spectrin repeat: a structural platform for cytoskeletal protein assemblies. FEBS Lett. 513:119-23 (2002).
5. Bennett V, Healy J. Organizing the fluid membrane bilayer: diseases linked to spectrin and ankyrin. Trends Mol. Med. 14:28-36 (2008).
6. Eber S, Lux SE. Hereditary spherocytosis–defects in proteins that connect the membrane skeleton to the lipid bilayer. Semin. Hematol. 41:118-41 (2004).
7. Mondello S, et al. αII-spectrin breakdown products (SBDPs): diagnosis and outcome in severe traumatic brain injury patients J. Neurotrauma 27:1203-13 (2010).