Secretin, alpha, Recombinant, Human (GST)

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 (2418 amino acids) consists of 22 repeating segments of about 106 amino acids in length. This protein was demonstrated to be a specific substrate for ubiquitina tion 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 sitedirected mutagenesis. Cell-free experiments using radiolabeled, biotinylated or native ubiquitin and cellular lysates from rabbit retyculocytes, human erythrocytes or k562 cells, showed that only monoubiquitination occurs at this site.\n\nDescription: \nRecombinant fusion protein: Glutathione-S-Transferase (GST) and a fragment of human a-spectrin (from Lysine 1601 to Leucine 1818) containing repeat 17 and the ubiquitination target lysine 27. The total molecular weight of the fusion protein is 52.4kD.\n\nApplication: \nSubstrate for cell-free ubiquitination assays.\n\nStability: \nrGST-alpha Spectrin although stable at 140C for 1 week, should be stored desiccated below -180C. Please prevent freeze-thaw cycles.

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SPECIFICATIONS

Catalog Number

S0625-15

Size

2ug

Form

Supplied as a liquid in 50mM Tris buffer, pH 8.0 and 10mM glutathione.

Purity

(same/more than) 90% as determined by both:\n(a) Analysis by RP-HPLC.\n(b) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.

References

1. A single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: analysis of the early stages of fibril formation.\n\nJ Mol Biol 2006 Feb 17;356(2):453-68\n\n2. A novel splicing mutation of the alpha-spectrin gene in the original hereditary pyropoikilocytosis kindred.\n\nBlood 2005 Dec 15;106(13):4367-9\n\n3. Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR.\n\nJ Biomol NMR 2005 Apr;31(4):295-310\n\n4. Mutational effects at the tetramerization site of nonerythroid alpha spectrin.\n\nBrain Res Mol Brain Res 2005 May 20;136(1-2):81-90\n\n5. Ubiquitination of red blood cell alpha-spectrin does not affect heterodimer formation.\n\nAm J Hematol 2005 Apr;78(4):281-7\n\n6. Pseudohypoaldosteronism type 1 and the genes encoding prostasin, alpha-spectrin, and Nedd4.\n\nInt J Mol Med 2004 Dec;14(6):1101-4