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Purification of His-tagged Proteins

Immobilized metal affinity chromatography (IMAC) is most frequently used for the purification of polyhistidine (His-) tagged proteins. This technique is based on the interaction between certain exposed protein residues (preferentially histidines) with transition metal cation Ni2+. Ni2+ itself is immobilized to a cross-linked agarose matrix via a chelating group such as nitrilotriacetic acid (NTA).

Nickel NTA Magnetic Agarose Beads

Ferrimagnetic agarose beads suitable for fast & efficient small-scale purification of polyhistidine (His) tagged proteins.

Nickel NTA Agaroses

6 % cross-linked agarose suitable for FPLC, gravity flow and batch purification by a one-step procedure from crude lysates both under denaturing and non-denaturing conditions

Selected References

[1] Porath et al. (1975) Metal chelate affinity chromatography, a new approach to protein fractionation. Nature 258:598.
[2] Gaberc-Porekar et al. (2001) Perspectives of immobilized-metal affinity chromatography. J. Biochem. Biophys. Methods 49:335.
[3] Ueda et al. (2003) Current and prospective applications of metal ion–protein binding. Journal of Chromatography 988:1.
[4] Liesiene et al. (1997) Immobilized metal affinity chromatography of human growth hormone-effect of ligand density. Journal of Chromatography 764:27.