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

15 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 the use of a simple capture affinity step on Amylose-Agarose or Dextrin-Sepharose columns, resulting in a protein that is often 70–90% pure in a single step. 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 paper 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.
Pages257-273
Number of pages17
DOIs
StatePublished - 2017

Publication series

NameMethods in Molecular Biology
Volume1485
ISSN (Print)1064-3745

Bibliographical note

Publisher Copyright:
© Springer Science+Business Media New York.

Keywords

  • Crystallization
  • Dextrin sepharose
  • Folding
  • Fusing protein tags
  • Maltose-binding protein
  • Protein aggregation and soluble aggregates
  • Protein expression and purifi cation
  • Protein solubility
  • Purifi cation techniques
  • TEV protease

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