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HaloLink™ Resin: High Capacity, Specificity and Scalable
Throughput for Protein Analysis
Marjeta Urh, Ph.D.1, Dan Simpson, Ph.D.1,
Jacqui Sankbeil, M.S.1, Danette Hartzell, Ph.D.1,
Natasha Karassina, M.S.1, Natalie Betz, Ph.D.1,
Nadine Nassif, M.S.1, Jami English, M.S.1, Ji
Zhu, Ph.D.2, Poncho Meisenheimer, Ph.D.2,
Dieter Klaubert, Ph.D.2, Bob Bulleit, Ph.D.1,
Keith Wood Ph.D.1
1Promega Corporation, 2Promega Biosciences, Inc.
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.
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