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HaloLink™ Resin: High Capacity, Specificity and Scalable Throughput for Protein Analysis

Marjeta Urh1, Dan Simpson1, Jacqui Sankbeil1, Danette Hartzell1, Natasha Karassina1, Natalie Betz1, Nadine Nassif1, Jami English1, Ji Zhu2, Poncho Meisenheimer2, Dieter Klaubert2, Bob Bulleit1, Keith Wood1
1Promega Corporation, 2Promega Biosciences, Inc.
Publication Date: 2006

Abstract

HaloLink™ Resin provides a new method for specific, covalent and oriented immobilization of proteins onto surfaces. The strategy is based on the HaloTag® Protein, which is derived from a catalytically inactive hydrolase engineered to form a covalent bond with a specific ligand. Here we demonstrate the high binding capacity and minimal nonspecific binding of the HaloLink™ Resin. We also show that the covalent HaloTag® bond provides stability during dilution and stringent washing, minimizing the loss of the HaloTag® fusion proteins from the surface. By analyzing protein:protein interactions and enzyme activity for several fusion proteins, we also demonstrate that fusion proteins bound to the HaloLink™ Resin maintain functionality. HaloLink™ Resin is not a purification resin; however, in conjunction with protease cleavage, it can be used to isolate a protein of interest.

Promega Notes 92, 24–29.

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