Shiga Like Toxin 1

Shiga Like Toxin-1 Subunit B Recombinant
Cat. No.
BT7044
Source
Escherichia Coli.
Synonyms
Appearance
Purity

Protein is >95% pure as determined by 10% PAGE (coomassie staining).

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Recombinant Shiga Like Toxin-1 Subunit B from E.Coli O157:H7 produced in E.coli containing amino acids 2-90 of the Shiga Like Toxin-1 Subunit B.
The Shiga Like Toxin 1 protein is fused to a 6xHis tag at its N-terminus and purified by proprietary chromatographic technique.

Product Specs

Introduction
Shiga-like toxin (verotoxin) is a toxin produced by certain Escherichia coli strains. Its name comes from its resemblance to the Shiga toxin (AB5-type) produced by Shigella dysenteriae bacteria. Two types are known: SLT1 and SLT2. This toxin is associated with hemolytic-uremic syndrome. To attach to and enter cells, Shiga-like toxin needs highly specific receptors on the cell surface. Animals like cattle, swine, and deer that lack these receptors can carry the toxigenic bacteria without experiencing illness. These animals then shed the bacteria in their feces, potentially spreading it to humans. Shiga Like Toxin-1 Subunit B, the functional region, binds to the receptor and has no toxic effects. It proves useful in vaccine research, antibody testing, and other functional studies.
Description
Recombinant Shiga Like Toxin-1 Subunit B, derived from E.Coli O157:H7, is produced in E.coli. This protein encompasses amino acids 2-90 of the Shiga Like Toxin-1 Subunit B and is fused to a 6xHis tag at its N-terminus. Purification is achieved through a proprietary chromatographic method.
Purity
The protein's purity exceeds 95%, as determined by 10% PAGE (coomassie staining).
Formulation
The protein is supplied in a solution of phosphate buffered saline with 50mM arginine at a pH of 7.4.
Stability
For use within 2-4 weeks, store the entire vial at 4°C. For longer storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Source
Escherichia Coli.
Purification Method

Purified by affinity chromatographic technique.

Product Science Overview

Introduction

Shiga-like toxins (SLTs), also known as verotoxins, are a family of related protein toxins produced by certain strains of bacteria, notably Shigella dysenteriae and Shiga-toxin-producing Escherichia coli (STEC) such as E. coli O157:H7. These toxins are responsible for causing severe gastrointestinal diseases, including bloody diarrhea and hemorrhagic colitis, which can sometimes lead to fatal systemic complications .

Structure and Function

Shiga-like toxins consist of two main components: the A subunit and the B subunit. The A subunit has RNA N-glycosidase activity, which inhibits eukaryotic protein synthesis, leading to cell death. The B subunit, on the other hand, forms a pentamer that binds to the functional cell-surface receptor globotriaosylceramide (Gb3). This binding is crucial for the toxin’s entry into the host cell .

Shiga Like Toxin-1 Subunit B Recombinant

The recombinant B subunit of Shiga-like Toxin-1 (SLT-1B) is a 7 kDa protein containing 69 amino acid residues. It is expressed in Escherichia coli and is used in various research applications due to its ability to bind specifically to Gb3 receptors. This specificity makes it a valuable tool for studying cell-specific vectorization, labeling, and imaging purposes .

Applications

The recombinant SLT-1B subunit has been utilized in several scientific studies and applications:

  1. Detection of Carbohydrate Ligands: The B subunit can be labeled with digoxigenin and used as a probe to detect carbohydrate ligands in immunochemical and flow cytometric applications. This allows for the measurement of carbohydrate binding activity in a simple and quantitative manner .
  2. Therapeutic and Vaccine Research: The specificity of SLT-1B for Gb3 receptors has been explored for its potential in therapeutic and vaccine research. By targeting Gb3-expressing cells, researchers aim to develop targeted therapies and vaccines that can neutralize the effects of Shiga-like toxins .
  3. Cell-Specific Vectorization: The ability of SLT-1B to bind specifically to Gb3 receptors overexpressed in tumor cells makes it a promising candidate for cell-specific vectorization. This can be used for targeted drug delivery and imaging in cancer research .

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