Monoclonal Anti-Maltose Binding Protein−Peroxidase antibody produced in mouse

Monoclonal Anti-Maltose Binding Protein (MBP) (mouse IgG1 isotype) is derived from the MBP-17 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from a BALB/c mouse immunized with purified recombinant MBP fusion protein. Maltose Binding Protein (MBP) is a periplasmic protein, which is specific to bacteria. It has maltodextrin binding site and binds to linear and cyclic maltodextrins. The mature MBP is produced from the pre-protein containing 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 Peroxidase antibody produced in mouse has been used in:

• immunoblotting
• dot blot
• enzyme-linked immunosorbent assay (ELISA)

Maltose Binding Protein (MBP) is often used to tag recombinant proteins to enhance the yield and facilitate the purification of the fusion product. Additionally, MBP tags can also improve the immunogenicity of the tagged protein. Thus, MBP can also be used as a carrier protein for vaccinations.

Maltose Binding Protein (MBP) mediates uptake of maltose. MBP is a substrate for chaperone secB. It has been reported that the addition of a maltose binding protein (MBP) tag creates a stable fusion product that does not appear to interfere with the bioactivity of the protein or with the biodistribution of the MBP tagged product.

Lyophilized in 0.01 M sodium phosphate buffered saline containing 1% bovine serum albumin and 0.05% MIT.

Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).

The antibody conjugate should be reconstituted with 0.5 mL deionized water.

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