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- W2181780724 abstract "Annexin V is a phospholipase A2. and protein kinase C inhibitory protein with calcium channel activity and an undefined role in cellular growth and differentiation. The proouct of annexin V gene is necessary for doing ex- periments to determine whether the tumor-associated annexin V protein can be used as a new molecular marker for diagnosis and prognosis of gastric carcinoma. This study describes the procedures which were used for cloning and expressing the human annexin Vasa maltose binding protein (MBP) fusion polypeptide in bacteria. The expres- sion plasmid for annexin V was constructed by ligation of the annexin V cDNA into the expression vector pMAL- c2x. The protein was expressed by E. coli strain TBl cells and purified by amylose affinity column chromato- graphy. The purity of the protein was assessed by SDS-PAGE and Western blot. The results showed that the molecular weight of the recombinant MBP-annexin V polypeptide was consistent with the calculated molecular weight, and that the purified protein appeared as an apparent single band of 77 kDa on the gel filtration column by SDS-PAGE. Our expression system allows the expression and purification of annexin V with MBP in high yield with no need of removal of the tag and gives pure protein in one purification step, and also makes it possible for the structural and functional studies of these proteins. (Life Science Journal. 2005; 2 ( l) : 22 - 26) (ISSN: 1097- 8135) ." @default.
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- W2181780724 date "2005-01-01" @default.
- W2181780724 modified "2023-09-27" @default.
- W2181780724 title "Expression and Purification of a Human Tumor-Associated Protein Annexin V" @default.
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