- Maltose-binding protein
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Maltose-Binding Protein (MBP) is a part of the maltose/maltodextrin system of Escherichia coli, which is responsible for the uptake and efficient catabolism of maltodextrins. It is a complex regulatory and transport system involving many proteins and protein complexes. MBP has an approximate molecular mass of 42.5 kilodaltons.
Use
MBP is used to increase the solubility of recombinant proteins expressed in E. coli. When the protein of interest is expressed as a MBP-fusion protein, its solubility is often enhanced, which is necessary for purification. The mechanism by which MBP increases solubility is not well understood. In addition, MBP can itself be used as an affinity tag for purification of recombinant proteins. The fusion protein binds to amylose columns while all other proteins flow through. The MBP-protein fusion can be purified by eluting the column with maltose. Once the fusion protein is obtained in purified form, the protein of interest (X) is often cleaved from MBP with a specific protease. Protein X can then be separated from MBP by ion exchange chromatography.
See Also
- Fluorescent glucose biosensors
- Glutathione S-transferase
External links
- N-Terminal Fusion of Target Protein to Maltose-Binding Protein at Michigan Technological University
- MeSH maltose-binding+protein
- Generic protocol for the expression and purification of recombinant proteins in Escherichia coli using a combinatorial His6-maltose binding protein fusion tag
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