MBP-probe Antibody (R3.2): sc-53366

MBP-probe Antibody (R3.2) is a mouse monoclonal IgG1 antibody that detects maltose binding protein (MBP) of non-species reactive (NSR) by western blotting (WB) and immunoprecipitation (IP). Anti-MBP antibody (R3.2) facilitates the study of MBP, a 370 amino acid protein derived from the E. coli malE gene, which plays a crucial role in the transport of maltose and maltodextrins across the bacterial cell membrane. MBP′s ability to bind maltose not only aids in nutrient uptake but also serves as a valuable tool in molecular biology for recombinant protein purification. MBP monoclonal antibody (R3.2) recognizes the MBP domain commonly utilized in fusion proteins, allowing for high-yield expression and straightforward purification through affinity chromatography with amylose resin. MBP′s importance extends beyond transport function, providing a means to visualize and isolate target proteins, making MBP an essential component in various experimental protocols. With the capability to be cleaved by coagulation factor Xa or eluted with excess maltose, MBP fusion proteins can be efficiently separated from their targets, enabling researchers to study protein interactions and functions in detail. MBP (R3.2) antibody′s versatility in applications such as western blotting (WB) and immunoprecipitation (IP) makes this reagent an indispensable tool for scientists investigating protein dynamics and interactions in their research.

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MBP-probe Antibody (R3.2) References:

1. Stimulation of the maltose transporter ATPase by unliganded maltose binding protein.  |  Gould, AD., et al. 2009. Biochemistry. 48: 8051-61. PMID: 19630440
2. Structure of an engineered β-lactamase maltose binding protein fusion protein: insights into heterotropic allosteric regulation.  |  Ke, W., et al. 2012. PLoS One. 7: e39168. PMID: 22720063
3. Competitive interactions of ligands and macromolecular crowders with maltose binding protein.  |  Miklos, AC., et al. 2013. PLoS One. 8: e74969. PMID: 24124463
4. High-yield soluble expression, purification and characterization of human steroidogenic acute regulatory protein (StAR) fused to a cleavable Maltose-Binding Protein (MBP).  |  Sluchanko, NN., et al. 2016. Protein Expr Purif. 119: 27-35. PMID: 26555181
5. Dynamical persistence of active sites identified in maltose-binding protein.  |  Nikolić, D. and Kovačev-Nikolić, V. 2017. J Mol Model. 23: 167. PMID: 28451879
6. Maltose chemoreceptor of Escherichia coli: interaction of maltose-binding protein and the tar signal transducer.  |  Kossmann, M., et al. 1988. J Bacteriol. 170: 4516-21. PMID: 3049536
7. Soluble Cytoplasmic Expression and Purification of Immunotoxin HER2(scFv)-PE24B as a Maltose Binding Protein Fusion.  |  Park, S., et al. 2021. Int J Mol Sci. 22: PMID: 34204265
8. Dependence of maltose transport and chemotaxis on the amount of maltose-binding protein.  |  Manson, MD., et al. 1985. J Biol Chem. 260: 9727-33. PMID: 3894359
9. The maltose-binding protein as a scaffold for monovalent display of peptides derived from phage libraries.  |  Zwick, MB., et al. 1998. Anal Biochem. 264: 87-97. PMID: 9784192
10. Model of maltose-binding protein/chemoreceptor complex supports intrasubunit signaling mechanism.  |  Zhang, Y., et al. 1999. Proc Natl Acad Sci U S A. 96: 939-44. PMID: 9927672

The preferred MBP-probe antibody is MBP-probe Antibody (R29.6): sc-13564.