glutathione S-transferase dynamin-1 fusion constructs are expressed in Escherichia coli BL21 cells, the proteins are purified using glutathione-Sepharose 4B beads
glutathione S-transferase-fused proteins are purified from Escherichia coli strain BL21 using glutathione-Sepharose, full-length dynamin is purified from rat brain
recombinant dynamin 1 GTPase domain GG1 from Escherichia coli strain BL21 (DE3) by glutathione affinity chromatography, tag cleavage by TEV protease, ultrafiltration, and gel filtration
recombinant GST- and His-tagged MxA from Escherichia coli strain BL21(DE3) by nickel affinity and glutathione affinity chromatography, and gel filtration
recombinant GST-tagged wild-type and mutant GST-SEY1 from Escherichia coli strain BL21 by glutathione affinity chromatography, the tag is cleaved off by thrombin
recombinant N-terminally Strep-tagged Drp1 from Escherichia coli strain BL21 Star (DE3) by affinity chromatography, followed by tag cleavage by HRV3C protease, and gel filtration
recombinant N-terminally Strep-tagged Drp1 from Saccharomyces cerevisiae strain JSY9612 by affinity chromatography, followed by tag cleavage by PreScission protease, and dialysis
recombinant nucleotide-free GTPase-GTPase effector domain fusion protein of human Drp1, and wild-type and mutant full-length enzymes from Escherichia coli strain BL21(DE3)