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Methods Mol Biol. 2011;681:281-93. doi: 10.1007/978-1-60761-913-0_15.

Purification of proteins fused to maltose-binding protein.

Author information

1
Protein Expression and Purification Facility, The Wolfson Centre for Applied Structural Biology, The Hebrew University of Jerusalem, Jerusalem, Israel.

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.

PMID:
20978971
DOI:
10.1007/978-1-60761-913-0_15
[Indexed for MEDLINE]

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