Recombinant Proteins

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MBP (27-392) E.Coli

Maltose Binding Protein E.coli Recombinant

Recombinant Maltose Binding Protein from E. coli is a single, non-glycosylated polypeptide chain. It contains 387 amino acids (residues 27-392), a 20 amino acid linker, and has a molecular weight of 42kDa.
Shipped with Ice Packs
Cat. No.
BT5593
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterilized by filtration.

MBP (27-396) E.Coli

Maltose Binding Protein (27-396) E.coli Recombinant

This recombinant E. coli MBP is produced in E. coli and consists of a single, non-glycosylated polypeptide chain. It contains 371 amino acids (specifically, amino acids 27-396) and has a molecular weight of 40.8 kDa. The MBP protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5669
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile filtered solution.

MBP E.Coli, His

Maltose Binding Protein E.coli Recombinant, His Tag

This recombinant E. coli MBP is produced in E. coli and consists of a single, non-glycosylated polypeptide chain. It contains 410 amino acids (specifically, amino acids 27 to 392) and has a molecular weight of 44.9kDa.
The MBP is linked to a 24 amino acid His-tag at its N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT5748
Source
Escherichia Coli.
Appearance
The solution is sterile, filtered, and colorless.
Definition and Classification

Maltose Binding Protein (MBP) is a part of the maltose/maltodextrin system of Escherichia coli (E. coli), which is responsible for the uptake and efficient catabolism of maltodextrins . MBP is a periplasmic binding protein that belongs to the family of periplasmic binding proteins (PBPs) and has an approximate molecular mass of 42.5 kilodaltons .

Biological Properties

Key Biological Properties: MBP is a monomeric protein encoded by the malE gene of E. coli. The malE gene codes for a precursor polypeptide (396 amino acid residues) which yields the mature MBP (370 residues) upon cleavage of the NH2-terminal extension . MBP is divided into two distinct globular domains connected by three short polypeptide segments, with a deep groove containing the maltose/maltodextrin binding site .

Expression Patterns and Tissue Distribution: MBP is exported into the periplasmic space of E. coli . The NH2-terminal extension, also termed signal peptide, directs the polypeptide to the membrane and SecYEG translocon .

Biological Functions

Primary Biological Functions: MBP plays a crucial role in the uptake and catabolism of maltodextrins in E. coli. It acts as a receptor for chemotaxis and gene regulation .

Role in Immune Responses and Pathogen Recognition: While MBP itself is not directly involved in immune responses, its role in the efficient uptake and utilization of maltodextrins can indirectly influence the metabolic state and overall fitness of E. coli, which can affect its interaction with the host immune system .

Modes of Action

Mechanisms with Other Molecules and Cells: MBP binds to maltose and maltodextrins, inducing a major conformational change that closes the groove by a rigid motion of the two domains around the linking polypeptide hinge . This binding is essential for the transport and metabolism of maltodextrins in E. coli .

Binding Partners and Downstream Signaling Cascades: MBP interacts with the maltose/maltodextrin transport system, including the MalFGK2 complex, to facilitate the transport of maltodextrins across the inner membrane .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The malE gene, coding for MBP, belongs to the Mal regulon of E. coli, which consists of ten genes geared for the efficient uptake and utilization of maltose and maltodextrins . The MalT protein activates transcription at all mal promoters, requiring maltotriose and ATP as ligands for binding to a dodecanucleotide MalT box upstream of all mal promoters .

Transcriptional Regulation and Post-Translational Modifications: The transcription activation performed by the MalT protein and the CRP-cAMP complex is connected with several regulation pathways implicated in sugar transport and adaptation to changes in osmolarity in the cell environment .

Applications

Biomedical Research: MBP is widely used as a fusion partner for producing recombinant proteins in bacterial cells. It enhances the solubility and proper folding of target proteins, making it a valuable tool in protein expression and purification .

Diagnostic Tools and Therapeutic Strategies: MBP fusion proteins are used in various diagnostic assays and therapeutic research due to their ability to enhance protein solubility and facilitate purification .

Role in the Life Cycle

Role Throughout the Life Cycle: MBP plays a critical role in the life cycle of E. coli by facilitating the uptake and metabolism of maltodextrins, which are essential for the bacterium’s growth and survival . Its function in chemotaxis and gene regulation also contributes to the bacterium’s ability to adapt to environmental changes .

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