|Cat. No. :
|Product Overview :
||Recombinant fusion protein: Glutathione-S-Transferase (GST) and a fragment of human α-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 52.4 kDa.
||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 and (280 and 246 kDa respectively). The human erithroid α-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 α-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.
|Physical Appearance :
||Sterile Filtered clear solution.
||Greater than 90.0% as determined by both: (a) Analysis by RP-HPLC. (b) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel
||The protein (1.7mg/ml) contains 50mM Tris buffer pH-8 and 10mM glutathione.
||Substrate for cell-free ubiquitination assays.
||rGST-alpha Spectrin although stable at 14℃ for 1 week, should be stored desiccated below -18℃. Please prevent freeze-thaw cycles.
||GST-a Spectrin; GST-alpha Spectrin.