Spectrin is a cytoskeletal protein that lines the intracellular side of the plasma membrane in eukaryotic cells. It was first isolated as a major protein component of human red blood cells which had been treated with mild detergent (Ghost RBC). Spectrin forms pentagonal or hexagonal arrangements, forming a scaffolding and playing an important role in maintenance of plasma membrane integrity and cytoskeletal structure. The hexagonal arrangements are formed by tetramers of spectrin subunits associating with short actin filaments at either end of the tetramer. These short actin filaments act as junctional complexes allowing the formation of the hexagonal mesh. The erythrocyte model demonstrates the importance of the spectrin cytoskeleton in that mutations in spectrin commonly cause hereditary defects of the erythrocyte, including hereditary elliptocytosis and hereditary spherocytosis. The spectrin gene family has undergone expansion during evolution. Rather than the one alpha and two beta genes in invertebrates, there are two alpha spectrins (alphaI and alphaII) and five beta spectrins (betaI to V), named in the order of discovery. In humans, the genes are: Alpha: SPTA1, SPTAN1 Beta: SPTB, SPTBN1, SPTBN2, SPTBN4, SPTBN5. Erythrocyte spectrin is the main component of the red cell membrane skeleton responsible for the shape and physical properties of red cells. Spectrin is composed of 2 subunits alpha and beta (280 and 246kD respectively). The human erithroid a-spectrin (2418aa) consists of 22 repeating segments of ~106aa in length. Spectrin repeats are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha- actinin, dystrophin and more recently the plakin family. The spectrin repeat forms a three-helix bundle. These conform to the rules of the heptad repeat. Spectrin repeats give rise to linear proteins. This protein was demonstrated to be a specific substrate for ubiquitination in vitro and in vivo. The main ubiquitination site on human a-spectrin was identified in the lysine 27 of the repeating segment 17 by site directed mutagenesis. Cell-free experiments using radiolabeled, biotinylated or native ubiquitin and cellular lysates from rabbit reticulocytes, human erythrocytes or k562 cells, showed that only monoubiquitination occurs at this site.||Source:|Recombinant protein corresponding to human a-Spectrin (from Lysine 160-Leucine 1818), containing repeat 17 and the ubiquitination target lysine 27, fused to GST-tag, expressed in E. coli.||Molecular Weight: |~52.4kD||AA Sequence:|A NLKQFYRDLE ELEEWISEML PTACDESYKD ATNIQRKYLK HQTFAHEVDG RSEQVHGVIN LGNSLIECSA CDGNEEAMKE QLEQLKEHWD HLLERTNDKG KKLNE||Applications: |Suitable for use as a substrate for cell-free ubiquitination assays. Other applications not tested.||Recommended Dilution:|Optimal dilutions to be determined by the researcher.||Storage and Stability:|May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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