Kate Qin Zhao, Rachel Friedman Ohana, Marjeta Urh, Jackie Kinney, John Eckert,
Lance Encell, and Keith Wood
To address the bottlenecks in over-expression and purification of soluble and functional proteins, we have developed HaloTag®, a 34 kDa, monomeric derivative of dehalogenase, engineered to enhance expression and solubility of recombinant proteins in E. coli and to provide efficient protein purification coupled with tag removal. When expressed as N-terminal HaloTag fusions in E. coli, target proteins can be produced at higher levels with higher solubility as compared to other fusion tags such as His(6)tag, GST and MBP. Target protein of higher yield, purity and free of tag is achieved using the HaloTag Protein Purification System through the covalent capture of the HaloTag protein onto HaloLink™ Resin and efficient target release by cleavage at an optimized TEV protease recognition site, leaving the HaloTag protein bound to the resin and pure protein in solution.
Do you have question about this Poster? Would you like more information about this poster?
Submit your questions here and BioTechniques will forward your question and contact information from our
database to an expert at