Purification of Proteins Fused to Maltose-Binding Protein

Mario Lebendiker*, Tsafi Danieli

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

32 Scopus citations


Maltose-binding protein (MBP) is one of the most popular fusion partners being used for producing recombinant proteins in bacterial cells. MBP allows one to use a simple capture affinity step on amylose–agarose columns, resulting in a protein that is often 70–90% pure. In addition to protein-isolation applications, MBP provides a high degree of translation and facilitates the proper folding and solubility of the target protein. This chapter describes efficient procedures for isolating highly purified MBP-target proteins. Special attention is given to considerations for downstream applications such as structural determination studies, protein activity assays, and assessing the chemical characteristics of the target protein.

Original languageAmerican English
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Number of pages13
StatePublished - 2011

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Bibliographical note

Funding Information:
We thank Dr. Erez Podoly from the Biological Chemistry Department of The Hebrew University of Jerusalem, now at the Structural Biology Department of Stanford University School of Medicine, for expressing the fusion protein, for his assistance with purification and his helpful suggestions. We thank Dr. Daria Mochly-Rosen from the Department of Chemical and Systems Biology, School of Medicine, Stanford University for kindly providing us with pMAL-c2MBP-Rack1.

Publisher Copyright:
© 2011, Springer Science+Business Media, LLC.


  • Amylose–agarose
  • Folding
  • Fusing protein tags
  • Maltose-binding protein
  • Protein aggregation and soluble aggregates
  • Protein expression and purification
  • Protein solubility
  • Purification techniques
  • TEV protease


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