Maltose Binding Protein (MBP) is a periplasmic protein specific to bacteria. It has maltodextrin binding site and binds to linear and cyclic maltodextrins. The mature MBP is synthesized from the pre-protein comprising of 26 amino acids, as signal peptide.
The antibody recognizes native as well as denatured-reduced forms of purified MBP and MBP fusion proteins.
Purified, recombinant MBP fusion protein
Endogenous intracellular levels of MBP in salmonella cells were determined by western blot analysis using a monoclonal anti-MBP antibody.
Monoclonal Anti-Maltose Binding Protein antibody produced in mouse has been used in the detection of MBP fusion protein using:
- western blotting and in vitro pull-down assay in Arabidopsis thaliana and Oryza sativa proteins
- dot blot assay of MBP recombinant G protein of Oryza sativa
- C3b complement component binding assay
Maltose Binding Protein (MBP) mediates uptake of maltose. MBP is a substrate for chaperone secB. Fusion of proteins with MBP tag at the N -terminus improves their solubility.
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