MBP E.Coli, His
Description
MBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
MBP often increases the production yield of its fusion partner and can improve the solubility of attached polypeptides.
The MBP is linked to a 24 amino acid His-tag at its N-terminus and purified using proprietary chromatographic methods.
Adding a carrier protein like 0.1% HSA or BSA is recommended for long-term storage.
Minimize repeated freezing and thawing.
Product Science Overview
Maltose Binding Protein (MBP) is a naturally occurring protein in Escherichia coli (E. coli), encoded by the malE gene. It plays a crucial role in the uptake, breakdown, and transport of maltodextrin, a carbohydrate. MBP is approximately 42 kDa in size and is widely used in recombinant protein expression systems due to its ability to enhance the solubility and stability of fusion proteins .
Recombinant MBP produced in E. coli is a single, non-glycosylated polypeptide chain containing 410 amino acids. It is often fused to a 24 amino acid His-tag at the N-terminus, which facilitates purification through affinity chromatography techniques . The His-tag, consisting of six histidine residues, allows for efficient binding to nickel or cobalt ions, making it easier to isolate the recombinant protein from the host cell lysate.
- Solubility Enhancement: One of the primary advantages of using MBP as a fusion partner is its ability to enhance the solubility of target proteins. This is particularly useful for proteins that are prone to forming insoluble aggregates, known as inclusion bodies, when overexpressed in E. coli .
- Stability: MBP is a stable monomer and does not promote protein aggregation. This makes it an ideal fusion partner for binding and cell adhesion studies .
- Versatility: MBP can be used in various expression systems, including mammalian cells, to enhance protein production. It has been shown to improve the yield and solubility of a wide range of proteins, including extracellular, intracellular, and transmembrane proteins .
MBP functions by binding to maltose and maltodextrins, facilitating their transport across the cell membrane. When used as a fusion partner, MBP helps to stabilize the target protein, preventing it from aggregating and enhancing its solubility. This is achieved through its highly soluble nature and ability to form stable monomers .
Recombinant MBP with a His-tag is widely used in research and biotechnology for the production of soluble and functional proteins. It is particularly useful in structural biology, where high-quality protein samples are required for crystallization and other biophysical studies. Additionally, MBP fusion proteins are used in various assays, including enzyme-linked immunosorbent assays (ELISAs) and Western blotting, due to their ease of purification and detection .
