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

35 Scopus citations

Abstract

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.
Pages281-293
Number of pages13
DOIs
StatePublished - 2011

Publication series

NameMethods in Molecular Biology
Volume681
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Bibliographical note

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

Keywords

  • 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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