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Immobilized metal ion affinity chromatography: a review on its applications

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TLDR
This review addresses the developments, limitations, and considerations of IMAC in the biopharmaceutical industry.
Abstract
After 35 years of development, immobilized metal ion affinity chromatography (IMAC) has evolved into a popular protein purification technique. This review starts with a discussion of its mechanism and advantages. It continues with its applications which include the purification of histidine-tagged proteins, natural metal-binding proteins, and antibodies. IMAC used in conjunction with mass spectroscopy for phosphoprotein fractionation and proteomics is also covered. Finally, this review addresses the developments, limitations, and considerations of IMAC in the biopharmaceutical industry.

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Citations
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Importance of the Support Properties for Immobilization or Purification of Enzymes

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Site-Specific PEGylation of Therapeutic Proteins.

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Recombinant protein production in bacterial hosts

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Challenges and opportunities in the purification of recombinant tagged proteins

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Label-Free Optical Biosensors Based on Aptamer-Functionalized Porous Silicon Scaffolds

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References
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Journal ArticleDOI

Metal chelate affinity chromatography, a new approach to protein fractionation

TL;DR: A highly flexible method based on affinities which can be used in a more selective fashion by modern chromatographic techniques is described here.
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Instability, stabilization, and formulation of liquid protein pharmaceuticals.

TL;DR: The basic behavior of proteins, their instabilities, and stabilization in aqueous state in relation to the development of liquid protein pharmaceuticals is discussed.
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New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues.

TL;DR: A novel nitrilotriacetic acid adsorbent has been prepared for metal chelate affinity chromatography and has been found to chelate Cu2+ and Ni2+ strongly and to be superior to the known iminodiacetic acid Adsorbent.
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Genetic Approach to Facilitate Purification of Recombinant Proteins with a Novel Metal Chelate Adsorbent

TL;DR: A general purification method for recombinant proteins based upon the selective interaction between a poly-histidine peptide, which is fused to the protein of interest, and a novel metal chelate adsorbent is described.
Journal ArticleDOI

Immobilized Gallium(III) Affinity Chromatography of Phosphopeptides

TL;DR: A novel procedure for micropurification of phosphorylated peptides, as a front end to mass spectrometric analysis, is described, and the use of an immobilized metal affinity chromatography (IMAC) in a microtip in combination with Ga(III) ions is proposed.
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