Purification of Proteins Fused to Maltose-Binding Protein

Mario Lebendiker; Tsafi Danieli

doi:10.1007/978-1-60761-913-0_15

Purification of Proteins Fused to Maltose-Binding Protein

Mario Lebendiker^*, Tsafi Danieli

^*Corresponding author for this work

Department of Biological Chemistry

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

37 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 language	English
Title of host publication	Methods in Molecular Biology
Publisher	Humana Press Inc.
Pages	281-293
Number of pages	13
DOIs	https://doi.org/10.1007/978-1-60761-913-0_15
State	Published - 2011

Publication series

Name	Methods in Molecular Biology
Volume	681
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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10.1007/978-1-60761-913-0_15

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Purification of Proteins Fused to Maltose-Binding Protein

Abstract

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