title: Expression and purification of recombinant human annexin V in Escherichia coli.
abstract: Human annexin V cDNA was cloned into plasmid pET19b and fused to a ten consecutive histidine tag at N-terminal. When expressed in E. coli BL21(DE3) LysS, the recombinant His10-annexin V accumulated in soluble form in the cytoplasm. By two-step chromatography, i.e., metal chelate affinity chromatography and anion exchange chromatography, recombinant His10-annexin V was purified to homogeneity on silver-stained SDS-PAGE gel. Recombinant annexin V, 7.4 mg, was obtained from a 1 litre flask culture.
authors.affiliation: Department of Biochemistry, Nanjing University, China.
authors.forename: L N
authors.initials: LN
authors.lastname: Zhang
authors.forename: X
authors.initials: X
authors.lastname: Yang
authors.forename: Z C
authors.initials: ZC
authors.lastname: Hua
mesh_terms: D017304:Annexin A5 / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D003001:Cloning, Molecular; D018076:DNA, Complementary; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D010957:Plasmids / Q000235:genetics* / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D017304:Annexin A5; D018076:DNA, Complementary; D011993:Recombinant Fusion Proteins