@inbook{41e7952a0f0b4c61a27bcd9ce7f94859,
title = "Purification of Proteins Fused to Maltose-Binding Protein",
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.",
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",
author = "Mario Lebendiker and Tsafi Danieli",
note = "Publisher Copyright: {\textcopyright} 2011, Springer Science+Business Media, LLC.",
year = "2011",
doi = "10.1007/978-1-60761-913-0_15",
language = "الإنجليزيّة",
series = "Methods in Molecular Biology",
pages = "281--293",
booktitle = "Methods in Molecular Biology",
}