For optical and phosphor-grade materials, where purities of 5 to 6 nines are required, the individual rare-earth element is initially purified by solvent extraction up to about 99.9 percent purity, and then it is further processed by ion exchange to reach the purity required for the given application.
The pristine MWCNTs were initially purified and treated with strong oxidizing acid following the previous method [8].
All GB1-fused UIM proteins were initially purified by a Ni2+-NTA column (Qiagen), followed by size-exclusion chromatography (Superdex-75, GE Healthcare).
Allatotropin (AT) was initially purified from the moth M. sexta as a 13-residue amidated peptide that strongly activates JH synthesis [57].
The fusion protein was initially purified by affinity chromatography on a HiTrap Chelating column (GE Healthcare) and then by ion exchange chromatography on a Mono Q column (GE Healthcare).
It was initially purified from LPS-stimulated human blood monocytes [2], [3] and it is now recognized that CXCL8 is produced by a wide range of cell types including non-immune cells, like fibroblasts and endothelial cells [4], [5].
The sAC protein was initially purified from rat testis cytosol, and two independent cDNAs, which were subsequently shown to represent alternatively spliced isoforms [4], were cloned from a rat testis cDNA library [2].
After incubation the samples were initially purified by ultracentrifugation (Beckman Coulter, L-90K ultracentrifuge) in a 50.2 Ti rotor at 42,000 rpm (3 hours, 4°C) and resuspended in 1 ml of the same buffer.
Soluble Mamu-DR αβ monomer secreted in supernatant from cloned S2 cells was initially purified by the Ni-NTA agarose, and then biotinylated enzymatically with the BirA enzyme at its optimal conditions.
The proteins were initially purified by GST tag affinity chromatography.
