MBP (27-396) E.Coli
Description
MBP protein was purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Maltose Binding Protein (MBP) is a periplasmic protein found in Escherichia coli (E. coli) that plays a crucial role in the transport and metabolism of maltose and maltodextrins. The recombinant form of MBP, specifically the segment spanning amino acids 27 to 396, is widely used in molecular biology and biochemistry for various applications, including protein purification and solubility enhancement.
MBP is encoded by the malE gene in E. coli. The full-length protein consists of 396 amino acids, but the recombinant form typically includes residues 27 to 396, resulting in a protein with a molecular mass of approximately 40.8 kDa . The protein is a monomer and does not contain any cysteine residues, which simplifies its folding and stability .
MBP is divided into two distinct globular domains connected by three short polypeptide segments. These domains create a deep groove that serves as the binding site for maltose and maltodextrins. The binding of maltose induces a significant conformational change in MBP, closing the groove and facilitating the transport of the sugar molecule .
Recombinant MBP is typically expressed in E. coli and purified using proprietary chromatographic techniques. The protein is produced as a single, non-glycosylated polypeptide chain and is often used in fusion with other proteins to enhance their solubility and prevent aggregation . The high purity (>95%) of the recombinant protein makes it suitable for various biochemical assays, including SDS-PAGE .
MBP is widely used as a fusion partner in recombinant protein expression systems. By fusing MBP to a target protein, researchers can take advantage of its solubility-enhancing properties, which help to prevent the aggregation of the target protein. This makes it easier to purify and study proteins that are otherwise difficult to express in a soluble form .
In addition to its use in protein purification, MBP is also employed in studies of protein-protein interactions, protein folding, and structural biology. Its ability to bind maltose and maltodextrins makes it a valuable tool for investigating carbohydrate-protein interactions and the mechanisms of sugar transport in bacteria .
