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Updated: Aug 5, 2026

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
Published on: January 16, 2012
A novel approach for purification of recombinant proteins using the dextran-binding domain
1Gene Discovery Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba, Japan. kaseda@nair.go.jp
Abstract:
Using the dextran-binding domain (DBD) of a type of glucosyltransferase (GTF) from Streptococcus sobrinus, we have developed a novel method for purifying recombinant proteins. DBD-tagged green and red fluorescent proteins as well as the parent GTF and DBD moiety were adsorbed well to commercially available cross-linked dextran (such as Sephadex beads and Sephacryl beads), and eluted efficiently with water-soluble dextran. The purity of the eluted proteins after this one-step affinity purification was approximately 90% or better. The results suggest that DBD can be used as a powerful carrier for purification of various recombinant proteins.

