|
Background
|
Maltose-Binding Protein (MBP) is a native E. coli protein and is part of a complex responsible for the uptake and efficient catabolism of maltodextrins. MBP is composed of 370 amino acid residues. As a fusion tag, MBP is useful for recombinant protein purification by affinity chromatography. It is also used to increase the expression level and solubility of the tagged protein, and for promoting proper folding of the attached protein. MBP increases solubility and the tag is thus particularly useful for recombinant proteins that may otherwise accumulate in an insoluble forms as inclusion bodies. Affinity purification takes place under physiological conditions and mild elution is performed using maltose. The mild elution conditions preserve the activity of the MBP-tagged protein.
|
