Mar 01, 2016 Ni/NiO core/shell nanoparticles for selective binding and magnetic separation of histidine-tagged proteins J. Am. Chem. Soc. , 128 ( 2006 ) , pp. 10658 - 10659 CrossRef View Record in Scopus Google Scholar
In previous studies, we synthesized the magnetic core-shell structured Fe 3 O 4 /PMG/IDA-Ni 2+ nanoparticles. The Ni 2+ on the surface of nanoparticles provides abundant docking sites for histidine, and the composite nanoparticles showed potential applications in the separation and purification of histidine-tagged (His-tagged) proteins. Meanwhile, the presence of the superparamagnetic core (Fe
Ni/NiO nanoparticles showed selective and efficient binding to histidine-tagged proteins and easy separation by using a magnet. These provided a more convenient way to efficient purification of histidine-tagged proteins compared with the conventional Ni-NTA
Highly selective magnetic affinity purification of histidine-tagged proteins by Ni2+ carrying monodisperse composite microspheres† Kouroush Salimi,a Duygu Deniz Usta,bc ˙Ilkay Ko er,a Eda elikad and Ali Tuncel*ae A magnetic sorbent with stable and superior magnetic behaviour was developed for His-tagged protein
His Mag Sepharose excel are Sepharose based magnetic beads designed for small-scale purification and expression screening of histidine-tagged proteins. These visible and dense beads allow convenient capture and handling of histidine-tagged proteins using a magnetic rack. Product Product code no. GE Data file code no. Pack size Approx. protein
The binding affinity of these contaminants is often lower than that of the tagged recombinant proteins; therefore, it may be possible to remove them by optimizing the separation conditions. The examples below show how changes in imidazole concentration during binding affect the purity of the histidine-tagged target protein
His Mag Sepharose Ni is a magnetic-bead-based IMAC medium charged with nickel ions. It is designed for efficient, small-scale purification/screening of histidine-tagged proteins from various sources. Histidine-tagged proteins are captured using immobilized nickel ions followed by collection of the beads using a magnetic device
Aug 01, 2021 Aug 01, 2021 Magnetic nanoparticles, decorated with these specific metal ions have proven to be very powerful sample separation and purification tools for histidine-tagged proteins . As we know, the purification of recombinant proteins is one of the most important requirements for downstream applications such as structural and functional studies
The magnetic core, with an average hydrodynamic size of 235.5 nm, allowed the magnetic nanoparticles (MNPs) rapid separation from solutions under an external magnetic field. NTA-Ni 2+ was modified on the surface of Fe 3 O 4 /PAM MNPs to selectively trap
Sep 07, 2021 In general, a novel magnetic nanomaterial basing on the coordination interaction between Ni 2+ and the carboxylates coated on the surface of Fe 3 O 4 nanoparticles was developed in this work, for fast and efficient His-tagged protein purification, which can be used to improve the separation of His-tagged protein from complex mixture
His Mag Sepharose Ni consists of Sepharose based magnetic beads designed for small-scale purification and expression screening of histidine-tagged proteins. These visible and dense beads allow convenient capture and simplified handling of histidine-tagged proteins using a magnetic rack
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