Highly Efficient Purification of Functional Proteins using HaloTag® Poster

Part # PS134

Abstract

Rachel Friedman Ohana, Robin Hurst, Jolanta Vidugiriene, Michael R. Slater, Marjeta Urh and Keith V. Wood
Promega Corporation, 2800 Woods Hollow Road, Madison, WI 53711

Although mammalian cells are preferred for producing functional mammalian proteins with appropriate post-translational modifications, purification of recombinant proteins is typically hampered by low expression levels. We have addressed this by creating a new method configured for mammalian cell culture, providing both rapid detection and efficient purification of mammalian proteins from their native environment. This approach is based on protein fusion tag (HaloTag®) and a series of ligands that form a highly specific and covalent bond with the HaloTag® protein. Ligands carrying a variety of functional groups, such as fluorescent molecules or surfaces, enable protein detection or covalent protein immobilization, respectively.

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