Anti-MBP [BBMBP23.42] Antibody
![Anti-MBP [BBMBP23.42] Antibody](https://www.kerafast.com/MediaStorage/Product/Images/Large/1046_2001202001263210450.jpg "Anti-MBP [BBMBP23.42] Antibody")
This mouse IgG2ak monoclonal antibody was raised against E.coli maltose binding protein (MBP) fusion construct and recognizes E. coli MBP.
Highlights:
- Reacts with E. coli MBP
- Binds to amino acid residues 27-392
- Suitable for Western Blot, Immunofluorescence and Immunocytochemistry applications
The E. coli maltose binding protein (MBP) is a product of the malE gene and is part of two multicomponent systems that uptake and sense maltose and higher-order glucose polymers (e.g. maltodextrin). MBP acts in the periplasmic space where it binds with high affinity to maltose/maltodextrin which, in turn binds to (i) a transport apparatus that translocates the MBP ligand across the inner membrane to the cytoplasm and (ii) chemoreceptors causing activation of a signaling pathway that directs taxis toward maltose. MBP is widely used as an affinity tag for purification of recombinant proteins. The reversible and high-affinity binding of MBP to amylose resins enables recovery of recombinant proteins at high purity in a single purification step. The purification and elution are performed under mild conditions, preserving the activity of the recombinant protein. In addition, MBP might increase expression, proper folding, and solubility, of its fusion partner.
From a laboratory at Agency for Science, Technology and Research (A*STAR).
This mouse IgG2ak monoclonal antibody was raised against E.coli maltose binding protein (MBP) fusion construct and recognizes E. coli MBP.
Highlights:
- Reacts with E. coli MBP
- Binds to amino acid residues 27-392
- Suitable for Western Blot, Immunofluorescence and Immunocytochemistry applications
The E. coli maltose binding protein (MBP) is a product of the malE gene and is part of two multicomponent systems that uptake and sense maltose and higher-order glucose polymers (e.g. maltodextrin). MBP acts in the periplasmic space where it binds with high affinity to maltose/maltodextrin which, in turn binds to (i) a transport apparatus that translocates the MBP ligand across the inner membrane to the cytoplasm and (ii) chemoreceptors causing activation of a signaling pathway that directs taxis toward maltose. MBP is widely used as an affinity tag for purification of recombinant proteins. The reversible and high-affinity binding of MBP to amylose resins enables recovery of recombinant proteins at high purity in a single purification step. The purification and elution are performed under mild conditions, preserving the activity of the recombinant protein. In addition, MBP might increase expression, proper folding, and solubility, of its fusion partner.
From a laboratory at Agency for Science, Technology and Research (A*STAR).
| Product Type: | Antibody |
| Accession ID: | P0AEX9, 914317 |
| Antigen: | MBP |
| Molecular Weight: | MBP precursor polypeptide 43 kDa, mature MBP 42 kDa |
| Isotype: | IgG2ak |
| Clonality: | Monoclonal |
| Clone Name: | BBMBP23.42 |
| Reactivity: | E. coli |
| Immunogen: | E.coli maltose binding protein (MBP) fusion construct |
| Species Immunized: | Mouse |
| Epitope: | Within MBP amino acid residues 27-392 |
| Purification Method: | Protein G |
| Buffer: | PBS, 0.05% (w/v) Sodium Azide |
| Tested Applications: | Western Blot and Immunofluorescence/Immunocytochemistry |
| Storage: | -20C |
| Shipped: | Cold Packs |
- Boos, W. & Shuman, H. Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation. Microbiol. Mol. Biol. Rev. 62, 204-29 (1998).
- Riggs, P. Expression and Purification of Maltose-Binding Protein Fusions. Curr. Protoc. Mol. Biol. Chapter 16, Unit16.6 (2001).
- Kapust, R. B. & Waugh, D. S. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8, 1668-1674 (1999).
- Kimple, M. E., Brill, A. L. & Pasker, R. L. Overview of affinity tags for protein purification. Curr. Protoc. Protein Sci. (2013).
If you publish research with this product, please let us know so we can cite your paper.
